Cellulase activity control by a terminator

ABSTRACT

The present invention relates to detergent compositions comprising a cellulase termination composition and cellulase in order to prevent potential tensile strength loss related to the hydrolytic activity of cellulase on cellulose substrates while maintaining the desired benefits from the use of cellulase.

FIELD OF THE INVENTION

The present invention relates to detergent compositions comprising acellulase termination composition and cellulase in order to preventpotential tensile strength loss related to the hydrolytic activity ofcellulase on cellulose substrates while maintaining the desired benefitsfrom the use of cellulase.

BACKGROUND OF THE INVENTION

The activity of cellulase is one in which cellulosic fibres orsubstrates are attacked by the cellulase and depending on the particularfunction of the cellulase, which can be endo-or exo cellulase and therespective hemicellulases. The cellulose structures are depolymerized orcleaved into smaller and thereby more soluble or dispersible fractures.This activity in particular on fabrics provides a cleaning,rejuvenation, softening and generally improved handfeel characteristicsto the structure. This has been previously speculated to be cleavage offibrils from the surface of fibres such that the main strand of thefibre becomes smoother, less available for incrustations, less likely toentangle with other fibers and optically less defuse in its lightreflecting and emission.

Naturally, improvements in the activity of particular cellulasecompositions have been made over time in order to allow lower usage orshorter exposure times for similar benefits. In the detergent fieldcellulases performing in a typical detergent wash environment areavailable with an activity at which the desired cellulase performance isreached prior to the end of a wash-cycle. However, since the cellulasecontinues to react, even after having provided the desired performance,cleavage of the cellulose will continue. Therefore, there is a potentialrisk of tensile strength loss. It should be noted however, tensilestrength loss of fabric is also an unavoidable result of mechanicalaction due to use/wearing and may further result from damage by ableaching component in the laundry process, especially if the fabric iscontaminated with metal compounds.

The obvious solution to the above problem is to use the appropriateamount of cellulase such that the time of a wash-cycle is coincidingwith the required time for the desired cellulase performance whiletensile strength loss is not yet occuring in a significant amount. Thishowever has proven difficult due to varying wash-cycles depending onlocal custom, washing machine equipment, cloths and soiling of thecloths be washed, additional additives incorporated into the detergentsfor other unrelated reasons and degradation of the cellulase uponstorage. Therefore a better way to provide the cellulase benefit whilepreventing fabric damage, is desirable.

According to the present invention, this is provided by including suchan amount of cellulase that the desired cellulase activity is certainlyachieved prior to the end of the wash-cycle while a cellulase terminatorprovides the means to prevent potential tensile strength loss withinthat time.

Cellulase exhibiting exceptionally high activity have been disclosed inthe context of compact detergents in WO-92-13057, in the context ofquaternary ammonium softening compounds in EP-A-495 554 and in thecontext of softening clay in a detergent composition in EP-A-495 258 andEP-A-177 165. Cellulase as such with exceptionally high activity hasbeen disclosed in WO 91/17243. Recognition of the potential tensilestrength loss of cellulase has been reported in several publications.For example Japanese application J-62-310754 discloses particularcellulases having a specific so-called non-degrading index. Japaneseapplication J-63-134830 discloses detergent compositions for clothingcontaining a cellulase which has a non-destructive index and U.S. Pat.No. 4,978,470 discloses a detergent composition for closing containingcellulase enzyme with a "non-degrading index" of less than 500.

The attempt to fine tune the cellulase activity to eliminate the problemunderlying the present invention as discussed above has its appeal morein the field of industrial cleaning where defined conditions inparticular length of fabric exposure to the cellulase, can be assumed.For the typical household conditions, the variation of individualsituations encountered, are so multiple that a high activity cellulasetogether with a terminator is a substantially better approach to ensurethe desired cellulase activity thereby preventing potential tensilestrength loss of the fabrics.

SUMMARY OF THE INVENTION

The present invention relates to the use of laundry detergentcompositions in household fabric treatment machines and handwashtreatments. The laundry detergent composition comprises a surface activesystem, a cellulase enzyme which preferably has a cellulase activity ofat least 10CEVU/l of liquid under treatment conditions and a cellulaseterminator composition satisfying the criteria of maximum 10% residualactivity in a standardized cellulase activity standard test such as theCMC viscosity reduction test and/or the cotton linter test. Thecellulase terminator composition is included in the laundry detergentcomposition at an amount such to control the activity of the cellulaseenzyme. The terminator composition used is a bleach terminatorcomprising a peroxidase with a bleaching system thereby preventingpotential tensile strength loss of the fibers. The terminatorcomposition is preferably in the laundry detergent composition in atime-delayed release form.

DETAILED DESCRIPTION OF THE INVENTION

Percentages used hereinafter are by weight unless otherwise stated.

CELLULASE

The activity of enzymes and particularly the activity of cellulaseenzyme has been defined for various applications by different analyticalmethods. These methods all attempt to provide a realistic assessment ofthe expected in use performance or at least a measurement correlatingwith the in use performance.

Even so there exist the various different tests for cellulase activity agenerally acceptable requirement for cellulase is a minimum viscosityreducing activity on CMC-solutions. Therefore the method of measuringthis so-called CMC Endoase activity (in units of 1 CEVU) will be usedherein for the preferred cellulases as explained below.

Cellulase preparations particularly useful in the compositions of theinvention are those which exhibit a CMC-endoase activity of at leastabout 10, preferably at least about 20 CEVU/l. In particular, apreferred cellulase exhibits a CMC-endoase activity of at least 25CEVU/l.

In the present context, the term "CMC-endoase activity" refers to theendoglucanase activity of the endoglucanase component in terms of itsability to degrade cellulose to glucose, cellobiose and triose, asdetermined by a viscosity decrease of a solution of carboxymethylcellulose (CMC) after incubation with the cellulase preparation of theinvention, as described in detail below.

The CMC-endoase (endoglucanase) activity can be determined from theviscosity decrease of CMC, as follows a substrate solution is prepared,containing 35 g/l CMC (Hercules 7 LFD) in 0.1 M tris buffer at pH 9.0.The enzyme sample to be analyzed is dissolved in the same buffer. 10mlsubstrate solution and 0.5 ml enzyme solution are mixed and transferredto a viscosimeter (e.g. Haake VT 181, NV sensor, 181 rpm), thermostatedat 40° C. Viscosity readings are taken as soon as possible after mixingand again 30 minutes later. The amount of enzyme that reduced theviscosity to one half under these conditions is defined as 1 unit ofCMC-endoase activity, or 1 CEVU/liter.

Another suitable method for testing the activities of the cellulase isthe cotton-linter method (see Example II).

The cellulases usable in the present invention include both bacterial orfungal cellulase. Preferably, they will have a pH optimum of between 5and 9.5. Suitable cellulases are disclosed in U.S. Pat. No. 4,435,307,Barbesgoard et al, which discloses fungal cellulase produced fromHumicola insolens. Suitable cellulases are also disclosed inGB-A-2.075.028; GB-A-2.095.275 and DE-OS-2.247.832.

Examples of cellulase components which may be usable in the presentinvention are:

A cellobiohydrolase component which is immunoreactive with an antibodyraised against a highly purified .sup.˜ 70kD cellobiohydrolase (EC3.2.1.91) derived from Humicola insolens, DSM 1800, or which is ahomologue or derivative of the .sup.˜ 70kD cellobiohydrolase exhibitingcellulase activity, or

an endoglucanase component which is immunoreactive with an antibodyraised against a highly purified .sup.˜ 50kD endoglucanase derived fromHumicola insolens, DSM 1800, or which is a homologue or derivative ofthe .sup.˜ 50kD endoglucanase exhibiting cellulase activity; a preferredendoglucanase component has the amino acid sequence disclosed in PCTPatent Application No. WO91/17244, or

an endoglucanase component which is immunoreactive with an antibodyraised against a highly purified .sup.˜ 50kD (apparent molecular weight,the amino acid composition corresponds to 45 kD with 2n glycosylationsites) endoglucanase derived from Fusarium oxysporum, DSM 2672, or whichis a homologue or derivative of the .sup.˜ 50kD endoglucanase exhibitingcellulase activity; a preferred endoglucanase component has the aminoacid sequence disclosed in PCT Patent Application No. WO91/17244, or anyof the cellulases disclosed in the published European Patent ApplicationNo. EP-A2-271 004, the cellulases having a non-degrading index (NDI) ofnot less than 500 and being alkalophilic cellulases having an optimum pHnot less than 7 or whose relative activity at a pH of not less than 8 is50% or over of the activity under optimum conditions when carboxy methylcellulose (CMC) is used as a substrate, or an endoglucanase componentwhich is immunoreactive with an antibody raised against a highlypurified .sup.˜ 43kD endoglucanase derived from Humicola insolens, DSM1800, or which is a homologue or derivative of the .sup.˜43 kDendoglucanase exhibiting cellulase activity; a preferred endoglucanasecomponent has the amino acid sequence disclosed in PCT PatentApplication No. WO 91/17243, or an endoglucanase component which isimmunoreactive with an antibody raised against a highly purified .sup.˜60kD endoglucanase derived from Bacillus lautus, NCIMB 40250, or whichis a homologue or derivative of the .sup.˜ 60kD endoglucanase exhibitingcellulase activity; a preferred endoglucanase component has the aminoacid sequence disclosed in PCT Patent Application No. WO 91/10732.

Especially suitable cellulases are the cellulases having color carebenefits. Examples of such cellulases are cellulases described inEuropean patent application No. 91202879.2, filed Nov. 6, 1991 (Novo).

According to the present invention, preferred cellulases are those asdescribed in Danish Patent Application 1159/90 or PCT patent applicationWO91/17243 which is also known as Carezyme(™) available from NovoNordisk A/S in Bagsvaerd, in Denmark. The cellulase preparationdescribed in these publications and the Carezyme(™) consistent with thisdescription, can consist essentially of a homogeneous endoglucanasecomponent, which is immunoreactive with an anti-body raised against ahighly purified 43 kD cellulase derived from Humicola Insulens, DSM1800, or which is homologous to said 43 kD endoglucanase. An alternativescreening for appropriate cellulases for use in the laundry detergentcomposition according to the present invention is the method specifiedin EP-A-495 258 or more specifically in EP-A-350 098.

For industrial production of the cellulase preparation herein, however,it is preferred to employ recombinant DNA techniques or other techniquesinvolving adjustments of fermentations or mutation of the microorganismsinvolved to ensure overproduction of the desired enzymatic activities.Such methods and techniques are known in the art and may readily becarried out by persons skilled in the art.

CELLULASE TERMINATOR COMPOSITION

The cellulase terminator composition comprises a peroxidase, an enhancerand a source of hydrogen peroxide which in combination act toirreversibly terminate the activity of the cellulase after a certaintime. The cellulase terminator composition will be referred to as CTChereinafter.

The function of the CTC is to control the activity of the cellulase insuch a way that the activity of the cellulase is more than 90% within 5minutes from the start of the wash cycle, the cellulase activity is lessthan 50% within 5 to 10 minutes from the start of the wash cycle andthat less than 10% of residual cellulase activity is reached after 15minutes in the wash cycle. The characteristics of the CTC in absence ofthe controlled release agent is that it reduces cellulase activity to10%, preferably 3% of the initial cellulase activity in a standardizedcotton linter test within 15 minutes of the wash cycle.

A preferred way to achieve the characteristic of the CTC is toincorporate one or more of the compounds of the CTC in a release agent.Said release agent is an agent which releases the incorporated CTCcompound into the wash environment in a controlled manner.

For example, the peroxidase is incorporated in a release agent such thatthe activity level of said peroxidase within 5 min of the wash cycle isless than 10%. More than 50% activity level of said peroxidase will bereached within the first 5-10 minutes from the start of the wash cycle.

Alternatively, said enhancer and/or said source of hydrogen peroxide maybe also incorporated independently into a release agent according to thepresent invention. In this case, said enhancer and/or said source ofhydrogen peroxide may be preferably incorporated independently in arelease agent. More preferably, said peroxidase and said enhancer may beincorporated together into a release agent according to the presentinvention, and said source of hydrogen peroxide may be incorporatedindependently into another release agent according to the presentinvention.

Preferably, said peroxidase is in the form of peroxidase-containinggranules (in the following sometimes denoted as "peroxidase granulate"or as "peroxidase-containing granulate). Said peroxidase granulate maysuitably further contain various granulation aids, binders, fillers,lubricants and the like. Examples hereof include cellulose (e.g.cellulose in fibre or microcrystalline form), dextrins (e.g. yellowdextrin), polyvinylpyrrolidone, polyvinylalcohol, cellulose derivatives(such as CMC or hydroxypropylcellulose), gelatin, salts (e.g. sodiumsulfate, sodium chloride, calcium sulfate or calcium carbonate),titanium dioxide, talc and clays (e.g. kaolin or bentonite). Othermaterials of relevance for incorporation in the granulates of the typein question are described, for example, in EP 0 304 331 B1, and will bewell known to persons skilled in the art. Said enhancer and said sourceof hydrogen peroxide may be also in the form of granulates. As apreferred option, when said enhancer is incorporated into a releaseagent, said peroxidase and said enhancer are granulated together forminga co-granulate to be incorporated into a release agent. Otherwise,independent enhancer-granulates and (source of hydrogenperoxide)-granulates may be also considered in the cleaning compositionaccording to the present invention.

Methods and apparatus for producing enzyme-containing granulates arelikewise well known to the skilled person (see, e.g. EP 0304 331 B1).Compact granulates--produced, e.g., using apparatus comprising knives asdescribed in Example 1 in U.S. Pat. No. 4,106,991--constitute verysuitable granulates (co-granulates) in the context of the presentinvention.

The release agent may be, for example, a coating. Said coating protectssaid granulates (co-granulates) in the wash environment for a certainperiod of time. The coating will normally be applied to said granulates(co-granulates) in an amount in the range of 0% to 50% by weight(calculated on the basis of the weight of the uncoated, dry granulate),preferably in the range of 5% to 40% by weight. The amount of coating tobe applied to said granulates will depend to a considerable extent onthe nature and composition of the desired coating, and to the kind ofprotection said coating should offer to said granulates. For example,the thickness of said coating or a multi-layered coating applied ontoany of the above granulates may determine the period in which thecontent of said granulates is released. A possible multi-layered coatingmay be a coating in which, for example, a fast release coating is coatedover a slow release coating.

Suitable release coatings are coatings which give rise to release of thecontents of the peroxidase- and/or enhancer (co-granulates) and/or(source of hydrogen peroxide)-granulates according to the presentinvention under the conditions prevailing during the use thereof. Thus,for example, when a preparation of the invention is to be introducedinto a washing liquor containing a washing detergent (normallycomprising, e.g. one or more types of surfactants), the coating shouldbe one which ensures the release of the contents of said granulates fromthe release agent when it is introduced into the washing medium.

Preferred release coating are coatings which are substantially insolublein water. Release coatings which are appropriate in washing media maysuitably comprise substances selected from the following: tallow;hydrogenated tallow; partially hydrolyzed tallow; fatty acids and fattyalcohols of natural and synthetic origin; long-chain fatty acid mono-,di- and triesters of glycerol (e.g. glycerol monostearate); ethoxylatedfatty alcohols; latexes; hydrocarbons of melting point in the range of50-80° C.; and waxes. Melt-coating agents are a preferred class of fastor slow release coating agents which can be used without dilution withwater. Reference may be made to Controlled Release Systems: FabricationTechnology, Vol. I, CRC Press, 1988, for further information on slowrelease coating.

Coatings may suitably further comprise substances such as clays (e.g.kaolin), titanium dioxide, pigments, salts (such as calcium carbonate)and the like. The person skilled in the art will be aware of furthercoating constituents of relevance in the present invention.

In the following, a preparation of a peroxidase-granulate incorporatedinto a release agent is described.

Granulation

2.0 kg of cellulose fibres (Arbocel™ BC 200), 0.9 kg of kaolin, 1.2 kgof yellow dextrin (TACKIDEX™ G155) and 10.1 kg of sodium sulfate (alldry components) were mixed in a Lodige mixer.

The above mixed dry components were sprayed, with continuous mixing,with 2.1 kg of liquid peroxidase concentrate (71 mg enzyme protein/g;Coprinus peroxidase produced as described in Example 1 in EP 505 311) towhich had been added (and dissolved) 0.5 kg of sucrose and 0.8 kg ofwater.

During and after spraying, a compact peroxidase-granulate was formed bymeans of the knives described in Example 1 in U.S. Pat. No. 4,106,991.

When the granulation was finished, the peroxidase-granulate was dried ona fluidized bed. The dry peroxidase-granulate was sieved, and theproduct fraction of size between 300 and 1000 mm was separated forcoating.

Coating

A peroxidase-granulate incorporated into a fast release agent is, forexample, an uncoated peroxidase-granulate. A peroxidase-granulateincorporated into a slow release agent may be made in the followingmanner. The peroxidase-granulate to be incorporated into a slow releaseagent was heated to 60° C. in a Lodige mixer, and 5% of glycerolmonostearate (also heated to 60° C.) was added under continuous mixing.When the glycerol monostearate was distributed, the peroxidase-granulatewas powdered with 6.7% of organoclay (Claytone™ AF) and 6.7% of titaniumdioxide under continuous mixing. All percentages are weight percentagesrelative to the dry uncoated peroxidase-granulate. After cooling, thecoated peroxidase-granulate, i.e. the peroxidase-granulate incorporatedinto slow release agent, was sieved and the fraction in the size range300-1100 mm was collected for use.

The CTC is used in the laundry detergent composition in an appropriateamount, preferably below 10% by weight. Naturally the "appropriateamount" strongly depends on the effectiveness of the CTC, the activityof the cellulase, the surfactant system and its interaction with thecellulase. Therefore the amount of CTC is a function of the othercompounds of the detergent composition and the washing conditions. Theamount in accordance with the present invention is selected such thatfor example in European washing conditions the cellulase activity of theselected cellulase is reduced to 10% of the initial cellulase within 15minutes from the start of the wash cycle.

CTC COMPOSITION

The CTC composition according to the present invention comprises aperoxidase, an enhancer and a source of hydrogen peroxidase.

Peroxidase enzymes (EC 1.11.1) employed in the context of the inventionmay very suitably be, e.g., any peroxidase comprised by the enzymeclassification EC 1.11.1.7; peroxidase fragments, exhibiting peroxidaseactivity, as well as synthetic or semi-synthetic peroxidase derivatives[e.g. with porphyrin ring systems], or microperoxidases (see, e.g., U.S.Pat. No. 4,077,768, EP 0 537 381, WO 91/05858 and WO 92/16634)] are alsorelevant in the context of the invention. Suitable peroxidases are knownfrom microbial, plant and animal origins. Other possible peroxidaseenzymes may be derived with protein engineering methods where one orseveral amino acids of the natural peroxidase enzyme may have beenreplaced by other amino acids.

Preferably, the peroxidase employed in the method of the presentinvention may be produced by plants (e.g. horseradish or soy beanperoxidase) or micro-organisms such as fungi or bacteria. Some preferredfungi include strains belonging to the subdivision Deuteromycotina,class Hyphomycetes, e.g. Fusarium, Humicola, Tricoderma, Myrothecium,Verticillum, Arthromyces, Caldariomyces, Ulocladium, Embellisia,Cladosprorium or Dreschlera, in particular Fusarium oxysporum (DSM2672), Humicola insolens, Trichoderma resii, Myrothecium verrucana (IFO6113), Verticillum alalboatrum, Verticillum dahlie, Arthromyces ramosus(FERM P-7754), Caldariomyces fumago, Ulocladium chartarum, Embellisiaalli or Dreschlera halodes.

Other preferred fungi include strains belonging to the subdivisionBasidiomycotina, class Basidiomycetes, e.g. Coprinus, Phanerochaete,Coriolus or Trametes, in particular Coprinus cinereus f. microsporus(IFO 8371), Coprinus macrorhizus, Phanerochaete chrysosporium (e.g.NA-12) or Trametes (previously called Polyporus), e.g. T. versicolor(e.g. PR428-A). Further preferred fungi include strains belonging to thesubdivision Zygomycotina, class Mycoraceae, e.g. Rhizopus or Mucor, inparticular Mucor hiemalis.

Some preferred bacteria include strains of the order Actinomycetales,e.g. Streptomyces spheroides (ATTC 23965), Streptomyces thermoviolaceus(IFO 12382) or Streptoverticillum verticillium ssp. verticillium. Otherpreferred bacteria include Bacillus pumilus (ATCC 12905), Bacillusstearothermophilus, Rhodobactersphaeroides, Rhodomonas palustri,Streptococcus lactis, Pseudomonas purrocinia (ATCC 15958) or Pseudomonasfluorescens (NRRL B-11). Further preferred bacteria include strainsbelonging to Myxococcus, e.g. M. virescens.

Other relevant peroxidases are "haloperoxidases" (see, e.g., U.S. Pat.No. 4,937,192), such as chloride peroxidases (EC 1.11.1.10), bromideperoxidases, and iodide peroxidases (EC 1.11.1.8). Other potentialsources of useful peroxidases are listed in B. C. Saunders et al.,Peroxidase, London, 1964, pp. 41-43.

The peroxidase may furthermore be one which may be produced by a methodcomprising cultivating a host cell transformed with a recombinant DNAvector which carries a DNA sequence encoding said peroxidase as well asDNA sequences encoding functions permitting the expression of the DNAsequence encoding the peroxidase, in a culture medium under conditionspermitting the expression of the peroxidase and recovering theperoxidase from the culture. Particularly, a peroxidase produced in arecombinant manner is a peroxidase derived from a Coprinus po., inparticular C. macrorhizus or C. cinereus according to WO 92/16634.

As already indicated to some extent above, the term peroxidase asemployed in the context of the invention embraces substances possessingperoxidase activity, such as peroxidase-active fragments derived fromcytochromes, hemoglobin or peroxidase enzymes, and synthetic orsemi-synthetic derivatives thereof, e.g. iron porphins, iron porphyrinsand iron phthalocyanine and derivatives thereof. The peroxidase employedin a preparation of the invention will very suitable often be a Coprinusperoxidase, a Myxococcus peroxidase, or a horseradish peroxidase.

Enhancers

The enhancer can be any suitable peroxidase enhancer. Examples ofenhancers include the following: halide ions (e.g. chloride andbromide); certain metal ions (e.g. Mn²⁺); phenolic species (e.g.p-hydroxycinnamic acid 2,4-dichlorophenol, vanillin, 7-hydroxycoumarin,6-hydroxy-2-naphtoic acid, and p-hydroxybenzenesulfonate); 2,2-azino-bis(3-ethylbenzothiazoline-6-sulfonate (ABTS; see, e.g., WO 94/12620); and10-methyl-, 10-ethyl- and 10-propyl-phenothiazine (see, e.g., WO94/12621). Numerous other enhancers or enhancing agents are disclosed inWO 94/12619, WO 94/12620 and WO 94/12621.

Preferred enhancers in the context of the present invention are10-phenothiazinepropionic acid (PPT), 10-ethylphenothiazine-4-carboxylicacid (EPC), 10-phenoxazinepropionic acid (POP) and 10-methylphenoxazine(described in WO 94/12621), and dye-transfer inhibitory co-granulatepreparations of the invention comprising such enhancers have goodstorage stability (shelf life), and lead to very satisfactorydye-transfer inhibition in fabric washing (vide infra).

Source of hydrogen peroxide

The bleaches suitable for the present invention include sources ofperoxygen bleaches. Examples of suitable sources of peroxygen bleachesinclude hydrogen peroxide releasing agents such as hydrogen peroxide,perborates, e.g. perborate monohydrate, perborate tetrahydrate,persulfates, percarbonates, peroxydisulfates, perphosphates andperoxyhydrates. Preferred bleaches are percarbonates and perborates.

The hydrogen peroxide releasing agents can be used in combination withbleach activators such as tetraacetylethylenediamine (TAED),nonanoyloxybenzene-sulfonate (NOBS, described in U.S. Pat. No.4,412,934), 3,5,5-trimethylhexanoloxybenzenesulfonate (ISONOES,described in EP 120,591), or pentaacetylglucose (PAG), which areperhydrolyzed to form a peracid as the active bleaching species, leadingto improved bleaching effect.

It may be also desirable to utilize an enzymatic process for hydrogenperoxide formation. Thus, the process according to the invention mayadditionally comprise adding an enzymatic system (i.e. an enzyme and asubstrate therefore) which is capable of generating hydrogen peroxideduring the washing process.

One such category of hydrogen peroxide generating systems comprisesenzymes which are able to convert molecular oxygen and an organic orinorganic substrate into hydrogen peroxide and the oxidized substraterespectively. These enzymes produce only low levels of hydrogenperoxide, but they may be employed to great advantage in the process ofthe invention as the presence of peroxidase ensures an efficientutilization of the hydrogen peroxide produced.

Preferred hydrogen peroxide-generating enzymes are those which act oncheap and readily available substrates which may conveniently beincluded into detergent compositions. An example of such a substrate isglucose which may be utilized for hydrogen peroxide production by meansof glucose oxidase. Suitable oxidases include those which act onaromatic compounds such as phenols and related substances. Othersuitable oxidases are urate oxidase, galactose oxidase, alcoholoxidases, amine oxidases, amino acid oxidase, amyloglucosidase, andcholesterol oxidase.

The preferred enzymatic systems are alcohol and aldehyde oxidases. Themore preferred systems for granular detergent application would havesolid alcohols, e.g. glucose whose oxidation is catalysed by glucoseoxidase to glucoronic acid with the formation of hydrogen peroxide. Themore preferred systems for liquid detergent application would involveliquid alcohols which could also act as, for example, solvents. Anexample is ethanol/ethanol oxidase. Such enzymatic systems are disclosedin EP Patent Application 91202655.6 filed Oct. 9, 1991.

Other peroxygen bleaches suitable for the present invention includeorganic peroxyacids such as percarboxylic acids.

Detergent Components

The detergent compositions of the invention may also contain additionaldetergent components. The precise nature of these additional components,and levels of incorporation thereof will depend on the physical form ofthe composition, and the nature of the cleaning operation for which itis to be used.

The compositions of the invention may for example, be formulated as handand machine laundry detergent compositions including laundry additivecompositions and compositions suitable for use in the pretreatment ofstained fabrics, rinse added fabric softener compositions, andcompositions for use in general household hard surface cleaningoperations.

When formulated as compositions suitable for use in a machine washingmethod, the compositions of the invention preferably contain both asurfactant and a builder compound and additionally one or more detergentcomponents preferably selected from organic polymeric compounds,bleaching agents, additional enzymes, suds suppressors, dispersants,lime-soap dispersants, soil suspension and anti-redeposition agents andcorrosion inhibitors. Laundry compositions can also contain softeningagents, as additional detergent components.

If needed the density of the laundry detergent compositions hereinranges from 550 to 1000 g/liter, preferably 600 to 950 g/liter ofcomposition measured at 20° C. The "compact" form of the compositionsherein is best reflected by density and, in terms of composition, by theamount of inorganic filler salt; inorganic filler salts are conventionalingredients of detergent compositions in powder form; in conventionaldetergent compositions, the filler salts are present in substantialamounts, typically 17-35% by weight of the total composition.

In the compact compositions, the filler salt is present in amounts notexceeding 15% of the total composition, preferably not exceeding 10%,most preferably not exceeding 5% by weight of the composition.

The inorganic filler salts, such as meant in the present compositionsare selected from the alkali and alkaline-earth-metal salts of sulphatesand chlorides.

A preferred filler salt is sodium sulphate.

Surfactant System

The detergent compositions according to the present invention comprise asurfactant system wherein the surfactant can be selected from nonionicand/or anionic and/or cationic and/or ampholytic and/or zwitterionicand/or semi-polar surfactants.

The surfactant is typically present at a level of from 0.1% to 60% byweight. More preferred levels of incorporation are 1% to 35% by weight,most preferably from 1% to 20% by weight of machine dishwashing, laundryand rinse added fabric softener compositions in accord with theinvention, and from 5% to 60% by weight, more preferably from 15% to 45%by weight of manual dishwashing compositions in accord with theinvention.

The surfactant is preferably formulated to be compatible with enzymecomponents present in the composition. In liquid or gel compositions thesurfactant is most preferably formulated such that it promotes, or atleast does not degrade, the stability of any enzyme in thesecompositions.

Preferred non-alkylbenzene sulfonate surfactant systems to be usedaccording to the present invention comprise as a surfactant one or moreof the nonionic and/or anionic surfactants described herein.

Polyethylene, polypropylene, and polybutylene oxide condensates of alkylphenols are suitable for use as the nonionic surfactant of thesurfactant systems of the present invention, with the polyethylene oxidecondensates being preferred. These compounds include the condensationproducts of alkyl phenols having an alkyl group containing from about 6to about 14 carbon atoms, preferably from about 8 to about 14 carbonatoms, in either a straight-chain or branched-chain configuration withthe alkylene oxide. In a preferred embodiment, the ethylene oxide ispresent in an amount equal to from about 2 to about 25 moles, morepreferably from about 3 to about 15 moles, of ethylene oxide per mole ofalkyl phenol. Commercially available nonionic surfactants of this typeinclude Igepal™ CO-630, marketed by the GAF Corporation; and Triton™X-45, X-114, X-100 and X-102, all marketed by the Rohm & Haas Company.These surfactants are commonly referred to as alkylphenol alkoxylates(e.g., alkyl phenol ethoxylates).

The condensation products of primary and secondary aliphatic alcoholswith from about 1 to about 25 moles of ethylene oxide are suitable foruse as the nonionic surfactant of the nonionic surfactant systems of thepresent invention. The alkyl chain of the aliphatic alcohol can eitherbe straight or branched, primary or secondary, and generally containsfrom about 8 to about 22 carbon atoms. Preferred are the condensationproducts of alcohols having an alkyl group containing from about 8 toabout 20 carbon atoms, more preferably from about 10 to about 18 carbonatoms, with from about 2 to about 10 moles of ethylene oxide per mole ofalcohol. About 2 to about 7 moles of ethylene oxide and most preferablyfrom 2 to 5 moles of ethylene oxide per mole of alcohol are present insaid condensation products. Examples of commercially available nonionicsurfactants of this type include Tergitol™ 15-S-9 (the condensationproduct of C₁₁ -C₁₅ linear alcohol with 9 moles ethylene oxide),Tergitol™ 24-L-6 NMW (the condensation product of C₁₂ -C₁₄ primaryalcohol with 6 moles ethylene oxide with a narrow molecular weightdistribution), both marketed by Union Carbide Corporation; Neodol™ 45-9(the condensation product of C₁₄ -C₁₅ linear alcohol with 9 moles ofethylene oxide), Neodol™ 23-3 (the condensation product of C₁₂ -C₁₃linear alcohol with 3.0 moles of ethylene oxide), Neodol™ 45-7 (thecondensation product of C₁₄ -C₁₅ linear alcohol with 7 moles of ethyleneoxide), Neodol™ 45-5 (the condensation product of C₁₄ -C₁₅ linearalcohol with 5 moles of ethylene oxide) marketed by Shell ChemicalCompany, Kyro™ EOB (the condensation product of C₁₃ -C₁₅ alcohol with 9moles ethylene oxide), marketed by The Procter & Gamble Company, andGenapol LA O5O (the condensation product of C₁₂ -C₁₄ alcohol with 5moles of ethylene oxide) marketed by Hoechst. Preferred range of HLB inthese products is from 8-11 and most preferred from 8-10.

Also useful as the nonionic surfactant of the surfactant systems of thepresent invention are the alkylpolysaccharides disclosed in U.S. Pat.No. 4,565,647, Llenado, issued Jan. 21, 1986, having a hydrophobic groupcontaining from about 6 to about 30 carbon atoms, preferably from about10 to about 16 carbon atoms and a polysaccharide, e.g. a polyglycoside,hydrophilic group containing from about 1.3 to about 10, preferably fromabout 1.3 to about 3, most preferably from about 1.3 to about 2.7saccharide units. Any reducing saccharide containing 5 or 6 carbon atomscan be used, e.g., glucose, galactose and galactosyl moieties can besubstituted for the glucosyl moieties (optionally the hydrophobic groupis attached at the 2-, 3-, 4-, etc. positions thus giving a glucose orgalactose as opposed to a glucoside or galactoside). The intersaccharidebonds can be, e.g., between the one position of the additionalsaccharide units and the 2-, 3-, 4-, and/or 6- positions on thepreceding saccharide units. The preferred alkylpolyglycosides have theformula

    R.sup.2 O(C.sub.n H.sub.2n O).sub.t (glycosyl).sub.x

wherein R² is selected from the group consisting of alkyl, alkylphenyl,hydroxyalkyl, hydroxyalkylphenyl, and mixtures thereof in which thealkyl groups contain from about 10 to about 18, preferably from about 12to about 14, carbon atoms; n is 2 or 3, preferably 2; t is from 0 toabout 10, preferably 0; and x is from about 1.3 to about 10, preferablyfrom about 1.3 to about 3, most preferably from about 1.3 to about 2.7.The glycosyl is preferably derived from glucose. To prepare thesecompounds, the alcohol or alkylpolyethoxy alcohol is formed first andthen reacted with glucose, or a source of glucose, to form the glucoside(attachment at the 1-position). The additional glycosyl units can thenbe attached between their 1-position and the preceding glycosyl units2-, 3-, 4- and/or 6-position, preferably predominately the 2-position.

The condensation products of ethylene oxide with a hydrophobic baseformed by the condensation of propylene oxide with propylene glycol arealso suitable for use as the additional nonionic surfactant systems ofthe present invention. The hydrophobic portion of these compounds willpreferably have a molecular weight of from about 1500 to about 1800 andwill exhibit water insolubility. The addition of polyoxyethylenemoieties to this hydrophobic portion tends to increase the watersolubility of the molecule as a whole, and the liquid character of theproduct is retained up to the point where the polyoxyethylene content isabout 50% of the total weight of the condensation product, whichcorresponds to condensation with up to about 40 moles of ethylene oxide.Examples of compounds of this type include certain of thecommercially-available Pluronic™ surfactants, marketed by BASF.

Also suitable for use as the nonionic surfactant of the nonionicsurfactant system of the present invention, are the condensationproducts of ethylene oxide with the product resulting from the reactionof propylene oxide and ethylenediamine. The hydrophobic moiety of theseproducts consists of the reaction product of ethylenediamine and excesspropylene oxide, and generally has a molecular weight of from about 2500to about 3000. This hydrophobic moiety is condensed with ethylene oxideto the extent that the condensation product contains from about 40% toabout 80% by weight of polyoxyethylene and has a molecular weight offrom about 5,000 to about 11,000. Examples of this type of nonionicsurfactant include certain of the commercially available Tetronic™compounds, marketed by BASF.

Preferred for use as the nonionic surfactant of the surfactant systemsof the present invention are polyethylene oxide condensates of alkylphenols, condensation products of primary and secondary aliphaticalcohols with from about 1 to about 25 moles of ethylene oxide,alkylpolysaccharides, and mixtures thereof. Most preferred are C₈ -C₁₄alkyl phenol ethoxylates having from 3 to 15 ethoxy groups and C₈ -C₁₈alcohol ethoxylates (preferably C₁₀ avg.) having from 2 to 10 ethoxygroups, and mixtures thereof.

Highly preferred nonionic surfactants are polyhydroxy fatty acid amidesurfactants of the formula. ##STR1## wherein R¹ is H, or R¹ is C₁₋₄hydrocarbyl, 2-hydroxy ethyl, 2-hydroxy propyl or a mixture thereof, R²is C₅₋₃₁ hydrocarbyl, and Z is a polyhydroxyhydrocarbyl having a linearhydrocarbyl chain with at least 3 hydroxyls directly connected to thechain, or an alkoxylated derivative thereof. Preferably, R¹ is methyl,R² is a straight C₁₁₋₁₅ alkyl or C₁₆₋₁₈ alkyl or alkenyl chain such ascoconut alkyl or mixtures thereof, and Z is derived from a reducingsugar such as glucose, fructose, maltose, lactose, in a reductiveamination reaction.

When included in such laundry detergent compositions, the nonionicsurfactant systems of the present invention act to improve thegreasy/oily stain removal properties of such laundry detergentcompositions across a broad range of laundry conditions.

Highly preferred anionic surfactants include alkyl alkoxylated sulfatesurfactants hereof are water soluble salts or acids of the formulaRO(A)_(m) SO3M wherein R is an unsubstituted C₁₀ -C₂₄ alkyl orhydroxyalkyl group having a C₁₀ -C₂₄ alkyl component, preferably a C₁₂-C₂₀ alkyl or hydroxyalkyl, more preferably C₁₂ -C₁₈ alkyl orhydroxyalkyl, A is an ethoxy or propoxy unit, m is greater than zero,typically between about 0.5 and about 6, more preferably between about0.5 and about 3, and M is H or a cation which can be, for example, ametal cation (e.g., sodium, potassium, lithium, calcium, magnesium,etc.), ammonium or substituted-ammonium cation. Alkyl ethoxylatedsulfates as well as alkyl propoxylated sulfates are contemplated herein.Specific examples of substituted ammonium cations include methyl-,dimethyl, trimethyl-ammonium cations and quaternary ammonium cationssuch as tetramethyl-ammonium and dimethyl piperdinium cations and thosederived from alkylamines such as ethylamine, diethylamine,triethylamine, mixtures thereof, and the like. Exemplary surfactants areC₁₂ -C₁₈ alkyl polyethoxylate (1.0) sulfate (C₁₂ -C₁₈ E(1.0)M), C₁₂ -C₁₈alkyl polyethoxylate (2.25) sulfate (C₁₂ -C₁₈ E(2.25)M), C₁₂ -C₁₈ alkylpolyethoxylate (3.0) sulfate (C₁₂ -C₁₈ E(3.0)M), and C₁₂ -C₁₈ alkylpolyethoxylate (4.0) sulfate (C₁₂ -C₁₈ E(4.0)M), wherein M isconveniently selected from sodium and potassium.

Suitable anionic surfactants to be used are alkyl ester sulfonatesurfactants including linear esters of C₈ -C₂₀ carboxylic acids (i.e.,fatty acids) which are sulfonated with gaseous O₀₃ according to "TheJournal of the American Oil Chemists Society", 52 (1975), pp. 323-329.Suitable starting materials would include natural fatty substances asderived from tallow, palm oil, etc. The preferred alkyl ester sulfonatesurfactant, especially for laundry applications, comprise alkyl estersulfonate surfactants of the structural formula: ##STR2## wherein R³ isa C₈ -C₂₀ hydrocarbyl, preferably an alkyl, or combination thereof, R⁴is a C₁ -C₆ hydrocarbyl, preferably an alkyl, or combination thereof,and M is a cation which forms a water soluble salt with the alkyl estersulfonate. Suitable salt-forming cations include metals such as sodium,potassium, and lithium, and substituted or unsubstituted ammoniumcations, such as monoethanolamine, diethanolamine, and triethanolamine.Preferably, R³ is C₁₀ -C₁₆ alkyl, and R⁴ is methyl, ethyl or isopropyl.Especially preferred are the methyl ester sulfonates wherein R³ is C₁₀-C₁₆ alkyl.

Other suitable anionic surfactants include the alkyl sulfate surfactantswhich are water soluble salts or acids of the formula ROSO₃ M wherein Rpreferably is a C₁₀ -C₂₄ hydrocarbyl, preferably an alkyl orhydroxyalkyl having a C₁₀ -C₂₀ alkyl component, more preferably a C₁₂-C₁₈ alkyl or hydroxyalkyl, and M is H or a cation, e.g., an alkalimetal cation (e.g. sodium, potassium, lithium), or ammonium orsubstituted ammonium (e.g. methyl-, dimethyl-, and trimethyl ammoniumcations and quaternary ammonium cations such as tetramethyl-ammonium anddimethyl piperdinium cations and quaternary ammonium cations derivedfrom alkylamines such as ethylamine, diethylamine, triethylamine, andmixtures thereof, and the like). Typically, alkyl chains of C₁₂ -C₁₆ arepreferred for lower wash temperatures (e.g. below about 50° C.) andC₁₆₋₁₈ alkyl chains are preferred for higher wash temperatures (e.g.above about 50° C.).

Other anionic surfactants useful for detersive purposes can also beincluded in the laundry detergent compositions of the present invention.These can include salts (including, for example, sodium, potassium,ammonium, and substituted ammonium salts such as mono-, di- andtriethanolamine salts) of soap, C₈ -C₂₂ primary of secondaryalkanesulfonates, C₈ -C₂₄ olefinsulfonates, sulfonated polycarboxylicacids prepared by sulfonation of the pyrolyzed product of alkaline earthmetal citrates, e.g., as described in British patent specification No.1,082,179, C₈ -C₂₄ alkylpolyglycolethersulfates (containing up to 10moles of ethylene oxide); alkyl glycerol sulfonates, fatty acyl glycerolsulfonates, fatty oleyl glycerol sulfates, alkyl phenol ethylene oxideether sulfates, paraffin sulfonates, alkyl phosphates, isethionates suchas the acyl isethionates, N-acyl taurates, alkyl succinamates andsulfosuccinates, monoesters of sulfosuccinates (especially saturated andunsaturated C₁₂ -C₁₈ monoesters) and diesters of sulfosuccinates(especially saturated and unsaturated C₆ -C₁₂ diesters), acylsarcosinates, sulfates of alkylpolysaccharides such as the sulfates ofalkylpolyglucoside (the nonionic nonsulfated compounds being describedbelow), branched primary alkyl sulfates, and alkyl polyethoxycarboxylates such as those of the formula RO(CH₂ CH₂ O)_(k) --CH₂COO--M+ wherein R is a C₈ -C₂₂ alkyl, k is an integer from 1 to 10, andM is a soluble salt-forming cation. Resin acids and hydrogenated resinacids are also suitable, such as rosin, hydrogenated rosin, and resinacids and hydrogenated resin acids present in or derived from tall oil.Further examples are described in "Surface Active Agents and Detergents"(Vol. I and II by Schwartz, Perry and Berch). A variety of suchsurfactants are also generally disclosed in U.S. Pat. No. 3,929,678,issued Dec. 30, 1975 to Laughlin, et al. at Column 23, line 58 throughColumn 29, line 23 (herein incorporated by reference). When includedtherein, the laundry detergent compositions of the present inventiontypically comprise from about 1% to about 40%, preferably from about 3%to about 20% by weight of such anionic surfactants.

It has been found that the CTC is very efficient at anionic/nonionicratio between 10:1 to 1:2.

The laundry detergent compositions of the present invention may alsocontain cationic, ampholytic, zwitterionic, and semi-polar surfactants,as well as the nonionic and/or anionic surfactants other than thosealready described herein. Cationic detersive surfactants suitable foruse in the laundry detergent compositions of the present invention arethose having one long-chain hydrocarbyl group. Examples of such cationicsurfactants include the ammonium surfactants such asalkyltrimethylammonium halogenides, and those surfactants having theformula:

    [R.sup.2 (OR.sup.3).sub.y ][(R.sup.4 (OR.sup.3).sub.y ].sub.2 R.sup.5 N+X-

wherein R² is an alkyl or alkyl benzyl group having from about 8 toabout 18 carbon atoms in the alkyl chain, each R³ is selected from thegroup consisting of --CH₂ CH₂ --, --CH₂ CH(CH₃)--, --CH₂ CH(CH₂ OH)--,--CH₂ CH₂ CH₂ --, and mixtures thereof; each R⁴ is selected from thegroup consisting of C₁ -C₄ alkyl, C₁ -C₄ hydroxyalkyl, benzyl ringstructures formed by joining the two R⁴ groups, --CH₂ CHOH--CHOHCOR⁶CHOHCH₂ OH wherein R⁶ is any hexose or hexose polymer having a molecularweight less than about 1000, and hydrogen when y is not 0; R⁵ is thesame as R⁴ or is an alkyl chain wherein the total number of carbon atomsof R² plus R⁵ is not more than about 18; each y is from 0 to about 10and the sum of the y values is from 0 to about 15; and X is anycompatible anion.

Highly preferred cationic surfactants are the water-soluble quaternaryammonium compounds useful in the present composition having the formula:

    R.sub.1 R.sub.2 R.sub.3 R.sub.4 N+X-(i)

wherein R₁ is C₈ -C₁₆ alkyl, each of R₂, R₃ and R₄ is independently C₁-C₄ alkyl, C₁ -C₄ hydroxy alkyl, benzyl, and --(C₂ H₄₀)_(x) H where xhas a value from 2 to 5, and X is an anion. Not more than one of R₂, R₃or R₄ should be benzyl. The preferred alkyl chain length for R₁ is C₁₂-C₁₅ particularly where the alkyl group is a mixture of chain lengthsderived from coconut or palm kernel fat or is derived synthetically byolefin build up or OXO alcohols synthesis.

Preferred groups for R₂ R₃ and R₄ are methyl and hydroxyethyl groups andthe anion X may be selected from halide, methosulphate, acetate andphosphate ions. Examples of suitable quaternary ammonium compounds offormulae (i) for use herein are:

coconut trimethyl ammonium chloride or bromide;

coconut methyl dihydroxyethyl ammonium chloride or bromide;

decyl triethyl ammonium chloride;

decyl dimethyl hydroxyethyl ammonium chloride or bromide;

C₁₂₋₁₅ dimethyl hydroxyethyl ammonium chloride or bromide;

coconut dimethyl hydroxyethyl ammonium chloride or bromide;

myristyl trimethyl ammonium methyl sulphate;

lauryl dimethyl benzyl ammonium chloride or bromide;

lauryl dimethyl (ethenoxy)₄ ammonium chloride or bromide;

choline esters (compounds of formula (i) wherein R₁ is CH₂ -CH₂--O--C--C₁₂₋₁₄ alkyl and R₂ R₃ R₄ are methyl). ##STR3## di-alkylimidazolines [compounds of formula (i)].

Other cationic surfactants useful herein are also described in U.S. Pat.No. 4,228,044, Cambre, issued Oct. 14, 1980 and in European PatentApplication EP 000,224.

When included therein, the laundry detergent compositions of the presentinvention typically comprise from 0.2% to about 25%, preferably fromabout 1% to about 8% by weight of such cationic surfactants. It has beenfound that the combination of cationic surfactants, cellulase and CTCleads to synergistic improvements in softening and cleaning.

Ampholytic surfactants are also suitable for use in the laundrydetergent compositions of the present invention. These surfactants canbe broadly described as aliphatic derivatives of secondary or tertiaryamines, or aliphatic derivatives of heterocyclic secondary and tertiaryamines in which the aliphatic radical can be straight- orbranched-chain. One of the aliphatic substituents contains at leastabout 8 carbon atoms, typically from about 8 to about 18 carbon atoms,and at least one contains an anionic water-solubilizing group, e.g.carboxy, sulfonate, sulfate. See U.S. Pat. No. 3,929,678 to Laughlin etal., issued Dec. 30, 1975 at column 19, lines 18-35, for examples ofampholytic surfactants.

When included therein, the laundry detergent compositions of the presentinvention typically comprise from 0.2% to about 15%, preferably fromabout 1% to about 10% by weight of such ampholytic surfactants.

Zwitterionic surfactants are also suitable for use in laundry detergentcompositions. These surfactants can be broadly described as derivativesof secondary and tertiary amines, derivatives of heterocyclic secondaryand tertiary amines, or derivatives of quaternary ammonium, quaternaryphosphonium or tertiary sulfonium compounds. See U.S. Pat. No. 3,929,678to Laughlin et al., issued Dec. 30, 1975 at column 19, line 38 throughcolumn 22, line 48, for examples of zwitterionic surfactants.

When included therein, the laundry detergent compositions of the presentinvention typically comprise from 0.2% to about 15%, preferably fromabout 1% to about 10% by weight of such zwitterionic surfactants.

Semi-polar nonionic surfactants are a special category of nonionicsurfactants which include water-soluble amine oxides containing onealkyl moiety of from about 10 to about 18 carbon atoms and 2 moietiesselected from the group consisting of alkyl groups and hydroxyalkylgroups containing from about 1 to about 3 carbon atoms; water-solublephosphine oxides containing one alkyl moiety of from about 10 to about18 carbon atoms and 2 moieties selected from the group consisting ofalkyl groups and hydroxyalkyl groups containing from about 1 to about 3carbon atoms; and water-soluble sulfoxides containing one alkyl moietyof from about 10 to about 18 carbon atoms and a moiety selected from thegroup consisting of alkyl and hydroxyalkyl moieties of from about 1 toabout 3 carbon atoms. Semi-polar nonionic detergent surfactants includethe amine oxide surfactants having the formula ##STR4## wherein R³ is analkyl, hydroxyalkyl, or alkyl phenyl group or mixtures thereofcontaining from about 8 to about 22 carbon atoms; R⁴ is an alkylene orhydroxyalkylene group containing from about 2 to about 3 carbon atoms ormixtures thereof; x is from 0 to about 3; and each R⁵ is an alkyl orhydroxyalkyl group containing from about 1 to about 3 carbon atoms or apolyethylene oxide group containing from about 1 to about 3 ethyleneoxide groups. The R⁵ groups can be attached to each other, e.g., throughan oxygen or nitrogen atom, to form a ring structure.

These amine oxide surfactants in particular include C₁₀ -C₁₈ alkyldimethyl amine oxides and C₈ -C₁₂ alkoxy ethyl dihydroxy ethyl amineoxides.

When included therein, the laundry detergent compositions of the presentinvention typically comprise from 0.2% to about 15%, preferably fromabout 1% to about 10% by weight of such semi-polar nonionic surfactants.

Optional Deterrent Ingredients:

Preferred detergent compositions of the present invention may furthercomprise an enzyme which provides cleaning performance and/or fabriccare benefits. Said enzymes include enzymes selected from proteases,gluco-amylases, amylases, lipases, cutinases, pectinases, reductases,oxidases, phenoloxidases, lipoxygenases, ligninases, pullulanases,tannases, pentosanases, malanases, β-glucanases, arabinosidases ormixtures thereof.

A preferred combination is a cleaning composition having cocktail ofconventional applicable enzymes like protease, amylase, lipase, cutinasein conjunction with one or more plant cell wall degrading enzymes.

Preferred commercially available protease enzymes include those soldunder the tradenames Alcalase, Savinase, Primase, Durazym, and Esperaseby Novo Nordisk A/S (Denmark), those sold under the tradename Maxatase,Maxacal and Maxapem by Gist-Brocades, those sold by GenencorInternational, and those sold under the tradename Opticlean and Optimaseby Solvay Enzymes. Also proteases described in our co-pendingapplication U.S. Ser. No. 08/136,797 can be included in the detergentcomposition of the invention. Protease enzyme may be incorporated intothe compositions in accordance with the invention at a level of from0.000% to 2% active enzyme by weight of the composition. It has beenfound that the combination of proteases, cellulase and CTC leads toimproved wool and silk rejuvenation caused by the CTC effect on theprotease.

Other preferred enzymes that can be included in the detergentcompositions of the present invention include lipases. Suitable lipaseenzymes for detergent usage include those produced by microorganisms ofthe Pseudomonas group, such as Pseudomonas stutzeri ATCC 19.154, asdisclosed in British Patent 1,372,034. Suitable lipases include thosewhich show a positive immunological cross-reaction with the antibody ofthe lipase, produced by the microorganism Pseudomonas fluorescent IAM1057. This lipase is available from Amano Pharmaceutical Co. Ltd.,Nagoya, Japan, under the trade name Lipase P "Amano," hereinafterreferred to as "Amano-P". Especially suitable lipases are lipases suchas M1 Lipase^(R) and Lipomax^(R) (Gist-Brocades) and Lipolase^(R) (Novo)which have found to be very effective when used in combination with thecompositions of the present invention. Also suitable are cutinases [EC3.1.1.50] which can be considered as a special kind of lipase, namelylipases which do not require interfacial activation. Addition ofcutinases to detergent compositions have been described in e.g.WO-A-88/09367 (Genencor). The lipases and/or cutinases are normallyincorporated in the detergent composition at levels from 0.0001% to 2%of active enzyme by weight of the detergent composition.

Amylases (& and/or β) can be included for removal of carbohydrate-basedstains. Suitable amylases are Termamy¹ R (Novo Nordisk), Fungamyl^(R)and BAN^(R) (Novo Nordisk). The above-mentioned enzymes may be of anysuitable origin, such as vegetable, animal, bacterial, fungal and yeastorigin. Said enzymes are normally incorporated in the detergentcomposition at levels from 0.0001% to 2% of active enzyme by weight ofthe detergent composition. Other suitable detergent ingredients that canbe added are enzyme oxidation scavengers which are described inCopending European Patent application 92870018.6 filed on Jan. 31, 1992.Examples of such enzyme oxidation scavengers are ethoxylatedtetraethylene polyamines.

The compositions according to the present invention may further comprisea builder system. Any conventional builder system is suitable for useherein including aluminosilicate materials, silicates, polycarboxylatesand fatty acids, materials such as ethylenediamine tetraacetate, metalion sequestrants such as aminopolyphosphonates, particularlyethylenediamine tetramethylene phosphonic acid and diethylene triaminepentamethylenephosphonic acid. Though less preferred for obviousenvironmental reasons, phosphate builders can also be used herein.

Suitable builders can be an inorganic ion exchange material, commonly aninorganic hydrated aluminosilicate material, more particularly ahydrated synthetic zeolite such as hydrated zeolite A, X, B, HS or MAP.

Another suitable inorganic builder material is layered silicate, e.g.SKS-6 (Hoechst). SKS-6 is a crystalline layered silicate consisting ofsodium silicate (Na₂ Si₂ O₅).

Suitable polycarboxylates containing one carboxy group include lacticacid, glycolic acid and ether derivatives thereof as disclosed inBelgian Patent Nos. 831,368, 821,369 and 821,370. Polycarboxylatescontaining two carboxy groups include the water-soluble salts ofsuccinic acid, malonic acid, (ethylenedioxy) diacetic acid, maleic acid,diglycollic acid, tartaric acid, tartronic acid and fumaric acid, aswell as the ether carboxylates described in German Offenlegenschrift2,446,686, and 2,446,687 and U.S. Pat. No. 3,935,257 and the sulfinylcarboxylates described in Belgian Patent No. 840,623. Polycarboxylatescontaining three carboxy groups include, in particular, water-solublecitrates, aconitrates and citraconates as well as succinate derivativessuch as the carboxymethyloxysuccinates described in British Patent No.1,379,241, lactoxysuccinates described in Netherlands Application7205873, and the oxypolycarboxylate materials such as2-oxa-1,1,3-propane tricarboxylates described in British Patent No.1,387,447.

Polycarboxylates containing four carboxy groups include oxydisuccinatesdisclosed in British Patent No. 1,261,829, 1,1,2,2-ethanetetracarboxylates, 1,1,3,3-propane tetracarboxylates and 1,1,2,3-propanetetracarboxylates. Polycarboxylates containing sulfo substituentsinclude the sulfosuccinate derivatives disclosed in British Patent Nos.1,398,421 and 1,398,422 and in U.S. Pat. No. 3,936,448, and thesulfonated pyrolysed citrates described in British Patent No. 1,082,179,while polycarboxylates containing phosphone substituents are disclosedin British Patent No. 1,439,000.

Alicyclic and heterocyclic polycarboxylates includecyclopentane-cis,cis,cis-tetracarboxylates, cyclopentadienidepentacarboxylates, 2,3,4,5-tetrahydro-furan-cis, cis,cis-tetracarboxylates, 2,5-tetrahydro-furan-cis -dicarboxylates,2,2,5,5-tetrahydrofuran-tetracarboxylates,1,2,3,4,5,6-hexane-hexacar-boxylates and and carboxymethyl derivativesof polyhydric alcohols such as sorbitol, mannitol and xylitol. Aromaticpoly-carboxylates include mellitic acid, pyromellitic acid and thephthalic acid derivatives disclosed in British Patent No. 1,425,343.

Of the above, the preferred polycarboxylates are hydroxycarboxylatescontaining up to three carboxy groups per molecule, more particularlycitrates.

Preferred builder systems for use in the present compositions include amixture of a water-insoluble aluminosilicate builder such as zeolite Aor of a layered silicate (SKS-6), and a water-soluble carboxylatechelating agent such as citric acid.

A suitable chelant for inclusion in the detergent compositions inaccordance with the invention is ethylenediamine-N,N'-disuccinic acid(EDDS) or the alkali metal, alkaline earth metal, ammonium, orsubstituted ammonium salts thereof, or mixtures thereof. Preferred EDDScompounds are the free acid form and the sodium or magnesium saltthereof. Examples of such preferred sodium salts of EDDS include Na₂EDDS and Na₄ EDDS. Examples of such preferred magnesium salts of EDDSinclude MgEDDS and Mg₂ EDDS. The magnesium salts are the most preferredfor inclusion in compositions in accordance with the invention. Saidchelants, in combination with cellulase and CTC, have found tosynergistically improve the cleaning performance.

Preferred builder systems include a mixture of a water-insolublealuminosilicate builder such as zeolite A, and a watersolublecarboxylate chelating agent such as citric acid. Other builder materialsthat can form part of the builder system for use in granularcompositions include inorganic materials such as alkali metalcarbonates, bicarbonates, silicates, and organic materials such as theorganic phosphonates, amino polyalkylene phosphonates and aminopolycarboxylates.

Other suitable water-soluble organic salts are the homo- or co-polymericacids or their salts, in which the polycarboxylic acid comprises atleast two carboxyl radicals separated from each other by not more thantwo carbon atoms. Combination of cellulase, CTC and the above polymersleads to significally reduced inorganic encrustation. Polymers of thistype are disclosed in GB-A-1,596,756. Examples of such salts arepolyacrylates of MW 2000-5000 and their copolymers with maleicanhydride, such copolymers having a molecular weight of from 20,000 to70,000, especially about 40,000.

Detergency builder salts are normally included in amounts of from 10% to80% by weight of the composition preferably from 20% to 70% and mostusually from 30% to 60% by weight.

Another optional ingredient is a suds suppressor, exemplified bysilicones, and silica-silicone mixtures. Silicones can be generallyrepresented by alkylated polysiloxane materials while silica is normallyused in finely divided forms exemplified by silica aerogels and xerogelsand hydrophobic silicas of various types. These materials can beincorporated as particulates in which the suds suppressor isadvantageously releasably incorporated in a water-soluble orwater-dispersible, substantially non-surface-active detergentimpermeable carrier. Alternatively the suds suppressor can be dissolvedor dispersed in a liquid carrier and applied by spraying on to one ormore of the other components.

A preferred silicone suds controlling agent is disclosed in Bartollotaet al. U.S. Pat. No. 3,933,672. Other particularly useful sudssuppressors are the self-emulsifying silicone suds suppressors,described in German Patent Application DTOS 2 646 126 published Apr. 28,1977. An example of such a compound is DC-544, commercially availablefrom Dow Corning, which is a siloxane-glycol copolymer. Especiallypreferred suds controlling agent are the suds suppressor systemcomprising a mixture of silicone oils and 2-alkyl-alcanols. Suitable2-alkyl-alkanols are 2-butyl-octanol which are commercially availableunder the trade name Isofol 12 R. Such suds suppressor system aredescribed in Copending European Patent application N 92870174.7 filed 10November, 1992.

Especially preferred silicone suds controlling agents are described inCopending European Patent application NO92201649.8. Said compositionscan comprise a silicone/silica mixture in combination with fumednonporous silica such as Aerosil^(R).

The suds suppressors described above are normally employed at levels offrom 0.001% to 2% by weight of the composition, preferably from 0.01% to1% by weight. Other components used in detergent compositions may beemployed, such as soil-suspending agents, soil-release agents, opticalbrighteners, abrasives, bactericides, tarnish inhibitors, coloringagents, and/or encapsulated or non-encapsulated perfumes.

Especially suitable encapsulating materials are water soluble capsuleswhich consist of a matrix of polysaccharide and polyhydroxy compoundssuch as described in GB 1,464,616.

Other suitable water soluble encapsulating materials comprise dextrinsderived from ungelatinized starch acid-esters of substituteddicarboxylic acids such as described in U.S. Pat. No. 3,455,838. Theseacid-ester dextrins are,preferably, prepared from such starches as waxymaize, waxy sorghum, sago, tapioca and potato. Suitable examples of saidencapsulating materials include N-Lok manufactured by National Starch.The N-Lok encapsulating material consists of a modified maize starch andglucose. The starch is modified by adding monofunctional substitutedgroups such as octenyl succinic acid anhydride.

Antiredeposition and soil suspension agents suitable herein includecellulose derivatives such as methylcellulose, carboxymethylcelluloseand hydroxyethylcellulose, and homo- or co-polymeric polycarboxylicacids or their salts. Polymers of this type include the polyacrylatesand maleic anhydride-acrylic acid copolymers previously mentioned asbuilders, as well as copolymers of maleic anhydride with ethylene,methylvinyl ether or methacrylic acid, the maleic anhydride constitutingat least 20 mole percent of the copolymer. These materials are normallyused at levels of from 0.5% to 10% by weight, more preferably from 0.75%to 8%, most preferably from 1% to 6% by weight of the composition.

Preferred optical brighteners are anionic in character, examples ofwhich are disodium4,4'-bis-(2-diethanolamino-4-anilino-s-triazin-6-ylamino)stilbene-2:2'disulphonate, disodium 4,-4'-bis-(2-morpholino-4-anilino-s-triazin-6-ylamino-stilbene-2:2'-disulphonate,disodium4,4'-bis-(2,4-dianilino-s-triazin-6-ylamino)stilbene-2:2'disulphonate,monosodium4',4"-bis-(2,4-dianilino-s-triazin-6ylamino)stilbene-2-sulphonate,disodium4,4'-bis-(2-anilino-4-(N-methyl-N-2-hydroxyethylamino)-s-triazin-6-ylamino)stilbene-2,2'-disulphonate,di-sodium4,4'-bis-(4-phenyl-2,1,3-triazol-2-yl)-stilbene-2,2'disuiphonate,di-so-dium4,4'bis(2-anilino-4-(1-methyl-2-hydroxyethylamino)-s-triazin-6-ylami-no)stilbene-2,2'disulphonate,sodium 2(stilbyl-4"-(naphtho-1',2':4,5)-1,2,3-triazole-2"-sulphonate and4,4'-bis(2-sulphostyryl)biphenyl. Highly preferred brighteners are thespecific brighteners of copending European Patent application No.95201943.8.

Other useful polymeric materials are the polyethylene glycols,particularly those of molecular weight 1000-10000, more particularly2000 to 8000 and most preferably about 4000. These are used at levels offrom 0.20% to 5% more preferably from 0.25% to 2.5% by weight. Thesepolymers and the previously mentioned homo- or co-polymericpolycarboxylate salts are valuable for improving whiteness maintenance,fabric ash deposition, and cleaning performance on clay, proteinaceousand oxidizable soils in the presence of transition metal impurities.

Soil release agents useful in compositions of the present invention areconventionally copolymers or terpolymers of terephthalic acid withethylene glycol and/or propylene glycol units in various arrangements.Examples of such polymers are disclosed in the commonly assigned U.S.Pat. Nos. 4,116,885 and 4,711,730 and European Published PatentApplication No. 0 272 033. A particular preferred polymer in accordancewith EP-A-0 272 033 has the formula:

    (CH.sub.3 (PEG).sub.43).sub.0.75 (POH).sub.0.25 [(T-PO).sub.2.8 (T-PEG).sub.0.4 ]T(PO-H).sub.0.25 ((PEG).sub.43 CH.sub.3).sub.0.75

where PEG is --(OC₂ H₄)O--,PO is (OC₃ H₆ O) and T is (pcOC₆ H₄ CO).

Also very useful are modified polyesters as random copolymers ofdimethyl terephthalate, dimethyl sulfoisophthalate, ethylene glycol and1-2 propane diol, the end groups consisting primarily of sulphobenzoateand secondarily of mono esters of ethylene glycol and/or propane-diol.The target is to obtain a polymer capped at both end by sulphobenzoategroups, "primarily", in the present context most of said copolymersherein will be end-capped by sulphobenzoate groups. However, somecopolymers will be less than fully capped, and therefore their endgroups may consist of monoester of ethylene glycol and/or propane 1-2diol, thereof consist "secondarily" of such species.

The selected polyesters herein contain about 46% by weight of dimethylterephthalic acid, about 16% by weight of propane -1.2 diol, about 10 byweight ethylene glycol about 13% by weight of dimethyl sulfobenzoic acidand about 15% by weight of sulfoisophthalic acid, and have a molecularweight of about 3.000. The polyesters and their method of preparationare described in detail in EPA 311 342. The combination of cellulase,CTC and polyesters have found to synergistically improve the whitenessand color maintenance.

Softening Agents

Fabric softening agents can also be incorporated into laundry detergentcompositions in accordance with the present invention. These agents maybe inorganic or organic in type. Inorganic softening agents areexemplified by the smectite clays disclosed in GB-A-1 400 898 and inU.S. Pat. No. 5,019,292. Organic fabric softening agents include thewater insoluble tertiary amines as disclosed in GB-A1 514 276 andEP-B011 340 and their combination with mono C₁₂ -C₁₄ quaternary ammoniumsalts are disclosed in EP-B-0 026 527 and EP-B-0 026 528 anddi-long-chain amides as disclosed in EP-B-0 242 919. Other usefulorganic ingredients of fabric softening systems include high molecularweight polyethylene oxide materials as disclosed in EP-A-0 299 575 and 0313 146.

Levels of smectite clay are normally in the range from 5% to 15%, morepreferably from 8% to 12% by weight, with the material being added as adry mixed component to the remainder of the formulation. Organic fabricsoftening agents such as the water-insoluble tertiary amines or dilongchain amide materials are incorporated at levels of from 0.5% to 5% byweight, normally from 1% to 3% by weight whilst the high molecularweight polyethylene oxide materials and the water soluble cationicmaterials are added at levels of from 0.1% to 2%, normally from 0.15% to1.5% by weight. These materials are normally added to the spray driedportion of the composition, although in some instances it may be moreconvenient to add them as a dry mixed particulate, or spray them asmolten liquid on to other solid components of the composition. It hasbeen found that the softeness performance of the combination ofcellulase and smectite clay and CTC is synergistically enhanced.

Dye Transfer Inhibition

The present invention also relates to a process for inhibiting dyetransfer from one fabric to another of solubilized and suspended dyesencountered during fabric laundering operations involving coloredfabrics. It has been found that the combination of cellulase, polymericdye transfer inhibiting agents and CTC leads to synergistic improvementin color whiteness and maintenance.

Polymeric Dye Transfer Inhibiting Agents

The detergent compositions according to the present invention alsocomprise from 0.001% to 10%, preferably from 0.01% to 2%, morepreferably from 0.05% to 1% by weight of polymeric dye transferinhibiting agents. Said polymeric dye transfer inhibiting agents arenormally incorporated into detergent compositions in order to inhibitthe transfer of dyes from colored fabrics onto fabrics washed therewith.These polymers have the ability to complex or adsorb the fugitive dyeswashed out of dyed fabrics before the dyes have the opportunity tobecome attached to other articles in the wash. Especially suitablepolymeric dye transfer inhibiting agents are polyamine N-oxide polymers,copolymers of N-vinylpyrrolidone and N-vinylimidazole,polyvinylpyrrolidone polymers, polyvinyloxazolidones andpolyvinylimidazoles or mixtures thereof. Addition of such polymers alsoenhances the performance of the enzymes.

a) Polyamine N-oxide Polymers

The polyamine N-oxide polymers suitable for use contain units having thefollowing structure formula: ##STR5## wherein P is a polymerisable unit,whereto the R--N--O group can be attached to or wherein the R--N---Ogroup forms part of the polymerisable unit or a combination of both.##STR6## R are aliphatic, ethoxylated aliphatics, aromatic, heterocyclicor alicyclic groups or any combination thereof whereto the nitrogen ofthe N-O group can be attached or wherein the nitrogen of the N-O groupis part of these groups.

The N-O group can be represented by the following general structures:##STR7## wherein R1, R2, and R3 are aliphatic groups, aromatic,heterocyclic or alicyclic groups or combinations thereof, x or/and yor/and z is 0 or 1 and wherein the nitrogen of the N-O group can beattached or wherein the nitrogen of the N-O group forms part of thesegroups.

The N-O group can be part of the polymerisable unit (P) or can beattached to the polymeric backbone or a combination of both. Suitablepolyamine N-oxides wherein the N-O group forms part of the polymerisableunit comprise polyamine N-oxides wherein R is selected from aliphatic,aromatic, alicyclic or heterocyclic groups. One class of said polyamineN-oxides comprises the group of polyamine N-oxides wherein the nitrogenof the N-O group forms part of the R-group. Preferred polyamine N-oxidesare those wherein R is a heterocyclic group such as pyrridine, pyrrole,imidazole, pyrrolidine, piperidine, quinoline, acridine and derivativesthereof. Another class of said polyamine N-oxides comprises the group ofpolyamine N-oxides wherein the nitrogen of the N-O group is attached tothe R-group.

Other suitable polyamine N-oxides are the polyamine oxides whereto theN--O group is attached to the polymerisable unit. Preferred class ofthese polyamine N-oxides are the polyamine N-oxides having the generalformula (I) wherein R is an aromatic, heterocyclic or alicyclic groupswherein the nitrogen of the N--O functional group is part of said Rgroup. Examples of these classes are polyamine oxides wherein R is aheterocyclic compound such as pyrridine, pyrrole, imidazole andderivatives thereof. Another preferred class of polyamine N-oxides arethe polyamine oxides having the general formula (I) wherein R arearomatic, heterocyclic or alicyclic groups wherein the nitrogen of theN--O functional group is attached to said R groups.

Examples of these classes are polyamine oxides wherein R groups can bearomatic such as phenyl.

Any polymer backbone can be used as long as the amine oxide polymerformed is water-soluble and has dye transfer inhibiting properties.Examples of suitable polymeric backbones are polyvinyls, polyalkylenes,polyesters, polyethers, polyamide, polyimides, polyacrylates andmixtures thereof.

The amine N-oxide polymers of the present invention typically have aratio of amine to the amine N-oxide of 10:1 to 1:1000000. However theamount of amine oxide groups present in the polyamine oxide polymer canbe varied by appropriate copolymerization or by appropriate degree ofN-oxidation. Preferably, the ratio of amine to amine N-oxide is from 2:3to 1:1000000. More preferably from 1:4 to 1:1000000, most preferablyfrom 1:7 to 1:1000000. The polymers of the present invention actuallyencompass random or block copolymers where one monomer type is an amineN-oxide and the other monomer type is either an amine N-oxide or not.The amine oxide unit of the polyamine N-oxides has a PKa<10, preferablyPKa<7, more preferred PKa<6. The polyamine oxides can be obtained inalmost any degree of polymerisation. The degree of polymerisation is notcritical provided the material has the desired water-solubility anddye-suspending power.

Typically, the average molecular weight is within the range of 500 to1000,000; preferably from 1,000 to 50,000, more preferably from 2,000 to30,000, most preferably from 3,000 to 20,000.

b) Copolymers of N-vinylpyrrolidone and N-vinylimidazole

The N-vinylimidazole N-vinylpyrrolidone polymers used in the presentinvention have an average molecular weight range from 5,000-1,000,000,preferably from 20,000-200,000.

Highly preferred polymers for use in detergent compositions according tothe present invention comprise a polymer selected from N-vinylimidazoleN-vinylpyrrolidone copolymers wherein said polymer has an averagemolecular weight range from 5,000 to 50,000 more preferably from 8,000to 30,000, most preferably from 10,000 to 20,000. The average molecularweight range was determined by light scattering as described in Barth H.G. and Mays J. W. Chemical Analysis Vol 113, "Modern Methods of PolymerCharacterization". Highly preferred N-vinylimidazole N-vinylpyrrolidonecopolymers have an average molecular weight range from 5,000 to 50,000;more preferably from 8,000 to 30,000; most preferably from 10,000 to20,000.

The N-vinylimidazole N-vinylpyrrolidone copolymers characterized byhaving said average molecular weight range provide excellent dyetransfer inhibiting properties while not adversely affecting thecleaning performance of detergent compositions formulated therewith. TheN-vinylimidazole N-vinylpyrrolidone copolymer of the present inventionhas a molar ratio of N-vinylimidazole to N-vinylpyrrolidone from 1 to0.2, more preferably from 0.8 to 0.3, most preferably from 0.6 to 0.4.

c) Polyvinylpyrrolidone

The detergent compositions of the present invention may also utilizepolyvinylpyrrolidone ("PVP") having an average molecular weight of fromabout 2,500 to about 400,000, preferably from about 5,000 to about200,000, more preferably from about 5,000 to about 50,000, and mostpreferably from about 5,000 to about 15,000. Suitablepolyvinylpyrrolidones are commercially vailable from ISP Corporation,New York, N.Y. and Montreal, Canada under the product names PVP K-15(viscosity molecular weight of 10,000), PVP K-30 (average molecularweight of 40,000), PVP K-60 (average molecular weight of 160,000), andPVP K-90 (average molecular weight of 360,000). Other suitablepolyvinylpyrrolidones which are commercially available from BASFCooperation include Sokalan HP 165 and Sokalan HP 12;polyvinylpyrrolidones known to persons skilled in the detergent field(see for example EP-A-262,897 and EP-A-256,696).

d) Polyvinyloxazolidones:

The detergent compositions of the present invention may also utilizepolyvinyloxazolidone as a polymeric dye transfer inhibiting agent. Saidpolyvinyloxazolidones have an average molecular weight of from about2,500 to about 400,000, preferably from about 5,000 to about 200,000,more preferably from about 5,000 to about 50,000, and most preferablyfrom about 5,000 to about 15,000.

e) Polyvinylimidazole:

The detergent compositions of the present invention may also utilizepolyvinylimidazole as polymeric dye transfer inhibiting agent. Saidpolyvinylimidazoles have an average about 2,500 to about 400,000,preferably from about 5,000 to about 200,000, more preferably from about5,000 to about 50,000, and most preferably from about 5,000 to about15,000.

Method of washing

The process described herein comprises contacting fabrics with alaundering solution in the usual manner and exemplified hereunder.

The process of the invention is conveniently carried out in the courseof the cleaning process. The method of cleaning is preferably carriedout at 5° C. to 95° C., especially between 10° C. and 60° C. The pH ofthe treatment solution is preferably from 7 to 11, especially from 7.5to 10.5. Highly preferred pH is between 9 to 10.5.

The following examples are meant to exemplify compositions of thepresent invention, but are not necessarily meant to limit or otherwisedefine the scope of the invention.

LAS: Sodium linear C₁₂ alkyl benzene sulphonate

TAS: Sodium tallow alkyl sulphate

XYAS: Sodium C_(1X) -C_(1Y) alkyl sulfate

SAS: C₁₂ -C₁₄ secondary (2,3) alkyl sulfate in the form of the sodiumsalt.

APG: Alkyl polyglycoside surfactant of formula C₁₂ -(glycosyl)_(x),where x is 1.5,

AEC: Alkyl ethoxycarboxylate surfactant of formula C₁₂ ethoxy (2)carboxylate.

SS Secondary soap surfactant of formula 2-butyl octanoic acid

25EY: A C₁₂ -C₁₅ predominantly linear primary alcohol condensed with anaverage of Y moles of ethylene oxide

45EY: A C₁₄ -C₁₅ predominantly linear primary alcohol condensed with anaverage of Y moles of ethylene oxide

XYEZS C_(1X) -C_(1Y) sodium alkyl sulfate condensed with an average of Zmoles of ethylene oxide per mole

Nonionic: C₁₃ -C₁₅ mixed ethoxylated/propoxylated fatty alcohol with anaverage degree of ethoxylation of 3.8 and an average degree ofpropoxylation of 4.5 sold under the tradename Plurafax LF404 by BASFGmbh

CFAA: C₁₂ -C₁₄ alkyl N-methyl glucamide

TFAA: C₁₆ -C₁₈ alkyl N-methyl glucamide.

Silicate: Amorphous Sodium Silicate (SiO₂ :Na₂ O ratio=2.0)

NaSKS-6: Crystalline layered silicate of formula δ-Na₂ Si₂ O₅

Carbonate: Anhydrous sodium carbonate

Phosphate: Sodium tripolyphosphate

MA/AA:Copolymer of 1:4 maleic/acrylic acid, average molecular weightabout 80,000

Polyacrylate: Polyacrylate homopolymer with an average molecular weightof 8,000 sold under the tradename PA30 by BASF GmbH

Zeolite A: Hydrated Sodium Aluminosilicate of formula Na₁₂ (AlO₂SiO₂)₁₂. 27H₂ O having a primary particle size in the range from 1 to 10micrometers

Zeolite MAP: Alkali metal alumino-silicate of the zeolite P type havinga silicon to aluminium ratio not greater than 1.33

Citrate: Tri-sodium citrate dihydrate

Citric: Citric Acid

Perborate: Anhydrous sodium perborate monohydrate bleach, empiricalformula NaBO₂. H₂ O₂

PB4: Anhydrous sodium perborate tetrahydrate

Percarbonate: Anhydrous sodium percarbonate bleach of empirical formula2Na₂ CO₃. 3H₂ O₂

TAED: Tetraacetyl ethylene diamine

Paraffin: Paraffin oil sold under the tradename Winog 70 by Wintershall.

Amylase: Amylolytic enzyme sold under the tradename Termamyl by NovoNordisk A/S

Lipase: Lipolytic enzyme sold under the tradename Lipolase, LipolaseUltra by Novo Nordisk A/S

Peroxidase: Peroxidase enzyme POD

Cellulase: Cellulosic enzyme sold under the tradename Carezyme orCelluzyme by Novo Nordisk A/S. Carezyme 1T (1000 CEVU/g) Celluzyme 1T(1000 CEVU/g)

CMC: Sodium carboxymethyl cellulose

HEDP: 1,1-hydroxyethane diphosphonic acid

DETPMP: Diethylene triamine penta (methylene phosphonic acid), marketedby Monsanto under the Trade name Dequest

PVP: Polyvinyl pyrrolidone polymer

EDDS: Ethylenediamine -N, N'-disuccinic acid, [S,S] isomer in the formof the sodium salt.

Suds Suppressor: 25% paraffin wax Mpt 50° C., 17% hydrophobic silica,58% paraffin oil.

Granular Suds Suppressor: 12% Silicone/silica, 18% stearyl alcohol, 70%starch in granular form

SCS: Sodium cumene sulphonate

CTC: Coprinus cinereus peroxidase 0.3 POXU/ml PPT 4 M PB1 0.5% withrelease agent (Glycerolstearate coating)

CTCI: 0.5% PB1 POD (2 PODU/ml) 50 M phenolsulfonate

Sulphate: Anhydrous sodium sulphate.

HMWPEO: High molecular weight polyethylene oxide

PGMS: Polyglycerol monostearate having a tradename of Radiasurf 248

TAE 25: Tallow alcohol ethoxylate (25)

PEG-6: Polyethylene glycol having a molecular weight of 600.

EXAMPLE 1

A granular detergent was prepared according to a composition withoutCTCI in example 6d. The POD granulates in CTCI were applied withoutrelease agent. The following wash tests were carried out:

Conditions:

Miele washing machine W756

40° C. wash cycle

water hardness: 15 grains/US gallon

detergent usage: 120 g per wash

pH=8.5 (in wash liquor)

load composition: 2 kg cotton/polycotton fabrics tracers to assess colorrejuvenation; tracers were pilled cotton fabrics

WFK 11A test fabrics to measure tensile strength loss. Cellulaseconcentration: 165 CEVU/l Carezyme IT

Fabrics were washed for 12 wash cycles and then assessed for colorrejuvenation and tensile strength. The CTCI system was added to the washafter 0 min (treatment B), 5 min (treatment C), 10 min (treatment D).

    ______________________________________                                                        Color      Tensile strength                                   Treatment       rejuvenation*                                                                            loss**                                             ______________________________________                                        A     no CTCI       3.5 psu    130                                            B     CTCI added after                                                                            1.9 psu     95                                                  0 min                                                                   C     CTCI added after                                                                            3.0 psu    105                                                  5 min                                                                   D     CTCI added after                                                                            3.7 psu    111                                                  10 min                                                                  E     (treatment w/o                                                                              reference  100                                                  cellulase and                                                                 CTCI)                                                                   ______________________________________                                         *0-4 panel score unit (Scheffe scale)                                         0 = no difference, 4 = big improvement compared to treatment E difference     of 0.8 is statistically significant at 95% confidence level                   **Normalised tensile strength loss: difference of 10% is statistically        significant at 95% confidence level.                                     

The test proves that treatments A, C, D deliver the same high colourrejuvenation benefits whereas treatment B is deficient.

Treatment A, however, leads to significantly higher tensile strengthloss than treatments C and D. The optimum release profile for the CTCIsystem therefore is between 5-10 minutes delivering equal benefit to Aand no meaningful increase in tensile strength loss versus anil-cellulase treatment E.

EXAMPLE 2

The following washing machine test was performed. The first treatmentcorresponds to a reference treatment where a level of cellulase of 10CEVU/L is tested in absence CTC. The treatment 2 has the same level ofcellulase and a CTC (described in 3). Treatment 3 is the same astreatment 2 except that the CTC is not controlled released. Cellulaseactivity is monitored during the test via a method described in (2).

    ______________________________________                                        Minutes in                  Cellulase .sup.(1) Activity.sup.(2)               the wash.sup.(4) :  Control in the wash                                       Treatment:                                                                              CTC.sup.(3)                                                                             Release 0-5    5-10 >10                                   ______________________________________                                        1         No        --      100    85   80                                    2         Yes       Yes     100    5    0                                     3         Yes       No       5     0    0                                     ______________________________________                                         .sup.(1) The cellulase is Carezyme ™ supplied by Novo Nordisk. Activit     of the enzyme granulate is 1000 Cevu/g.                                       .sup.(2) The cellulase activity is quantified in a detergent matrix (5) b     a twostep procedure. The 1-4 glycoside bonds of insoluble cellulose           (cotton linters) are hydrolysed randomly by the cellulase in the presence     of cellobiase, to yield DGlucose. The concentration of Dglucose, which is     proportional to the cellulase activity is measured indirectly by              spectrophotometry at 340 nm using an Abbott commercial enzymatic testkit      (hexokinase and glucose6-phosphate  #dehydrogenase in the presence of         NAD+. Standard Carezyme ™ is used for calibration and the results are      expressed as % of standard Carezyme ™.                                     .sup.(3) Description of the: CTC system: Peroxidase derived from Coprinus     cinereous is suppiied by Novo Nordisk. The concentration of peroxidase        enzyme in the wash is 0.3 POXU/ml. The peroxidase enzyme is delivered in      the form of a control release granulate (activity of the granulate is 30      KPOXU/g). The enhancer is PPT (phenothiazine10-propionic acid). The           concentration of PPT accelerator is 4 μM, concentration of PB1 in the      wash is 35 ppm.  #Source of hydrogen peroxide is perborate monohydrate        (PB1).                                                                        .sup.(4) Test conditions: The granular detergent is added via an              granulette to a Miele washing machine. Detergent (6) concentration in the     wash liquor is 8000 ppm. Wash conditions are as follows: water temperatur     is 40° C., water hardness is 8 grain/US gallon. Tests are run in       absence of load.                                                              .sup.(5) The composition of the detergent used in the test is described i     the table below. Nonionic surfactant system used is a 2.7:1 mixture of        Marlipal 24/50 (C24EO5) and C16/C18 glucose amide. HLB of these surfactan     has been measured to be ≧10. The pH of the detergent has been          measured in the wash to be 9.5.                                          

    ______________________________________                                                        % by                                                                          weight of                                                                     the total                                                                     formula                                                       ______________________________________                                        45AS              8.5                                                         25E3S             2.1                                                         24E5              7.1                                                         C16/C18 glucose amide                                                                           2.6                                                         Zeolite           23.1                                                        Citrate           7.7                                                         citric acid       5.3                                                         Na-SKS-6          7.5                                                         Carbonate         3.1                                                         Bicarbonate       4.0                                                         Sulfate           5.94                                                        Polyacrylate      5.1                                                         CMC               0.36                                                        PVNO/PVPVI        0.19                                                        Protease          0.87                                                        Lipase            0.24                                                        Amylase           0.8                                                         EDDS              0.5                                                         Suds suppresser   0.41                                                        Water and miscellaneous                                                                         Balance                                                     ______________________________________                                    

The test results show that reference treatment 1 has relatively stablecellulase activity in the wash. Treatment 2 which incorporates thecontrolled release CTC, shows full cellulase activity for the first 5minutes of the wash. After 5 minutes, the CTC is released anddeactivates the cellulase. Treatment 3 however, shows a significant lossof cellulase activity right from the start of the wash. As a result,treatment 3 is deficient. Therefore, treatment 2 which contains thecontrolled release CTC is highly desired because it leads to optimumcellulase activity through the wash.

EXAMPLE 3

The following multi-cycle washing machine test was carried out under thelaundry conditions described in (5). The first treatment corresponds toa reference treatment where a level of cellulase of 10 CEVU/L is testedin absence CTC. The treatment 2 has a 5X higher level of cellulase and aCTC (described in 3). Treatment 3 is the same as treatment 2 except thatit does not incorporate the CTC. Tensile strength loss and depillingbenefits on cotton fabrics are monitored during the test.

    ______________________________________                                                Cellulase.sup.(1)     Depilling                                       Treatment                                                                             level (CEVU/L)                                                                            CTC (2)   benefits.sup.(3)                                                                     TSL.sup.(4)                              ______________________________________                                        1 (ref.)                                                                              10          no        4.0    100                                      2       50          yes       1.6    107                                      3       50          no        1.4    150                                      ______________________________________                                         .sup.(1) The cellulase is Carezyme ™ supplied by Novo Nordisk. Activit     of the enzyme granulate is 1000 Cevu/g.                                       .sup.(2) Description of the CTC system: Peroxidase derived from Coprinus      cinereous is supplied by Novo Nordisk. The concentration of peroxidase        enzyme in the wash is 0.3 POXU/ml. The peroxidase enzyme is delivered in      the form of a control release granulate (activity of the granulate is 30      KPOXU/g). The enhancer is PPT (phenothiazine10-propionic acid). The           concentration of PPT accelerator is 4 μM,  #concentration of PB1 in th     wash is 35 ppm. Source of hydrogen peroxide is perborate monohydrate          (PB1).                                                                        .sup.(3) Depilling benefits are determined by visual grading performed on     cotton socks which have been prewashed 10 times with detergent to create      pills on the surface. Depilling is measured after 6 wash cycles. Depillin     is measured on a scale from 1 (complete removal of pills) to 5 (high leve     of pills). A difference in pill grade which is ≧1 is considered        significant.                                                                  .sup.(4) Normalized tensile strength loss (TSL) is measured on                standardised fabrics on an Instron instrument. In the above example,          treatment 1 is the reference (100), the force necessary to break a piece      of fabrics which has been washed 30 times (i.e. 30 wash cycles). Wash         conditions are described in (5). A difference which is >10% is considered     significant.                                                                  .sup.(5) Test conditions: The granular detergent is added via an              granulette to a Miele washing machine. Detergent (6) concentration in the     wash liquor is 8000 ppm. Wash conditions are as follows: water temperatur     is 40° C., water hardness is 8 grain/US gallon. Tests are run in       the presence of a 3kg load of clean fabrics (polyester, cotton,               polycotton).                                                                  .sup.(6) The composition of the detergent used in the test is described i     the table below. Nonionic surfactant system used is a 2.7:1 mixture of        Marlipal 24/50 (C24EO5) and C16/C18 glucose amide. HLB of these surfactan     has been measured to be ≧10. The pH of the detergent has been          measured in the wash to be 9.5.                                          

(1) The cellulase is Carezyme™ supplied by Novo Nordisk. Activity of theenzyme granulate is 1000 Cevu/g.

(2) Description of the CTC system: Peroxidase derived from Coprinuscinereous is supplied by Novo Nordisk. The concentration of peroxidaseenzyme in the wash is 0.3 POXU/ml. The peroxidase enzyme is delivered inthe form of a control release granulate (activity of the granulate is 30KPOXU/g). The enhancer is PPT (phenothiazine-10-propionic acid). Theconcentration of PPT accelerator is 4 μM, concentration of PB1 in thewash is 35 ppm. Source of hydrogen peroxide is perborate mono-hydrate(PB1).

(3) Depilling benefits are determined by visual grading performed oncotton socks which have been pre-washed 10 times with detergent tocreate pills on the surface. Depilling is measured after 6 wash cycles.Depilling is measured on a scale from 1 (complete removal of pills) to 5(high level of pills). A difference in pill grade which is ≧1 isconsidered significant.

(4) Normalized tensile strength loss (TSL) is measured on standardisedfabrics on an Instron instrument. In the above example, treatment 1 isthe reference (100), the force necessary to break a piece of fabricswhich has been washed 30 times (i.e. 30 wash cycles). Wash conditionsare described in (5). A difference which is >10% is consideredsignificant.

(5) Test conditions: The granular detergent is added via an granuletteto a Miele washing machine. Detergent (6) concentration in the washliquor is 8000 ppm. Wash conditions are as follows: water temperature is40° C., water hardness is 8 grain/US gallon. Tests are run in thepresence of a 3-kg load of clean fabrics (poly-ester, cotton,polycotton).

(6) The composition of the detergent used in the test is described inthe table below. Non-ionic surfactant system used is a 2.7:1 mixture ofMarlipal 24/50 (C24EO5) and C16/C18 glucose amide. HLB of thesesurfactant has been measured to be ≧10. The pH of the detergent has beenmeasured in the wash to be 9.5.

    ______________________________________                                                       % by weight of                                                                the total                                                                     formula                                                        ______________________________________                                        45AS             8.5                                                          25E3S            2.1                                                          24E5             7.1                                                          C16/C18 glucose amide                                                                          2.6                                                          Zeolite          23.1                                                         Citrate          7.7                                                          citric acid      5.3                                                          Na-SKS-6         7.5                                                          Carbonate        3.1                                                          Bicarbonate      4.0                                                          Sulfate          5.94                                                         Polyacrylate     5.1                                                          CMC              0.36                                                         PVNO/PVPVI       0.19                                                         Protease         0.87                                                         Lipase           0.24                                                         Amylase          0.8                                                          EDDS             0.5                                                          Suds suppresser  0.41                                                         Water and miscellaneous                                                                        Balance                                                      ______________________________________                                    

The test results shows that reference treatment 1 delivers a relativelylow level of benefits. The benefit profile of treatment 1 is deficientcompared to the high level of benefit seen in treatment 2 and 3.Treatment 3 however, shows a significant level of TSL compared totreatment 1 and 2. As a result, treatment 3 is deficient. Therefore,treatment 2 which contains the CTC is highly desired for benefits andbecause it is not deficient in the risk area.

EXAMPLE 4

Granular fabric cleaning compositions in accordance with the inventionwere prepared as follows:

    ______________________________________                                                     I     II       III    IV                                         ______________________________________                                        LAS            22.0    22.0     22.0 22.0                                     Phosphate      30.0    23.0     23.0 23.0                                     Carbonate/Bicarbonate**                                                                      23.0    23.0     23.0 23.0                                     Silicate       14.0    14.0     14.0 14.0                                     Zeolite A      --       8.2     8.2  8.2                                      DETPMP         0.4     0.4      0.4  0.4                                      MA/AA          1.0     0.5      1.0  1.0                                      Sodium Sulfate 5.5     5.5      5.5  5.5                                      * Protease     0.01    0.02     0.01 0.005                                    * Lipolytic enzyme(s)                                                                        0.005   0.01     --   0.01                                     * Cellulase (1000 CEVU/g)                                                                    0.3     0.5      0.8  0.3                                      * Amylase      0.01    --       0.01 0.006                                    * Pectinase    0.02    0.02     0.02 --                                       * Xylanase     0.01                                                           CTC            +       +        +    +                                        Water/minors   Up to 100%                                                     ______________________________________                                         *The level of enzyme(s) is by weight of "pure" enzyme                         **to control pH                                                          

EXAMPLE 5

Granular fabric cleaning compositions in accordance with the inventionwere prepared as follows:

    ______________________________________                                                    I    II       III     IV                                          ______________________________________                                        LAS           12.0   12.0     12.0  12.0                                      Zeolite A     26.0   26.0     26.0  26.0                                      SS            4.0    4.0      4.0   4.0                                       SAS           5.0    5.0      5.0   5.0                                       Citrate/Citric acid**                                                                       10.0   10.0     10.0  10.0                                      Sodium Sulfate                                                                              20.0   20.0     20.0  30.0                                      MA/AA         1.5    1.5      --     --                                       AA            --     --       1.0   --                                        * Protease    0.06   0.03     0.02  0.08                                      * Lipolytic enzyme(s)                                                                       --     0.01     0.005 0.01                                      * Cellulase   0.5    0.8      0.4   0.8                                       * Amylase     --     0.01     0.01  0.005                                     * Pectinase   --     --       0.02  0.01                                      * Xylanase    --     --       0.02  --                                        CTC           +      +        +     +                                         Water/minors  Up to 100%                                                      ______________________________________                                         *The level of enzyme(s) is by weight of "pure" enzyme                         **to control pH                                                          

EXAMPLE 6

Granular fabric cleaning compositions in accordance with the inventionwhich are especially useful in the laundering of coloured fabrics wereprepared as follows:

    ______________________________________                                                      A    B        C       D                                         ______________________________________                                        LAS             11.4   10.7     --    11                                      TAS             1.8    2.4      --    5                                       TFAA            --     --       4.0   --                                      45AS            3.0    3.1      10.0  --                                      45E7            4.0    4.0      --    6                                       25E3S           --     --       3.0   --                                      68E11           1.8    1.8      --    --                                      25E5            2.0    --       8.0   --                                      Citrate/Citric acid**                                                                         17.0   17.5     10.0  21                                      Carbonate       --     --       10    5                                       Zeolite A       32.5   32.1     25.0  32                                      Na-SKS-6        --     --       9.0   --                                      MA/AA           5.0    5.0      5.0   4.0                                     DETPMP          1.0    0.2      0.8   0.2                                     * Protease      0.02   0.02     0.01  0.02                                    * Lipolytic enzyme(s)                                                                         0.03   0.04     0.005 0.04                                    * Amylase       --     0.03     0.005 0.01                                    * Pectinase     --     --       0.01  --                                      * Cellulase     0.8    0.8      0.8   2.5                                     * Xylanase      --     --       0.02  --                                      Silicate        2.0    2.5      --    2.0                                     Sulphate        3.5    5.2      3.0   5.0                                     PVP             0.3    0.5      --    0.3                                     Poly (4-vinylpyridine)-N-                                                                     --     --       0.2   --                                      oxide/copolymer of vinyl-                                                     imidazole and vinyl-                                                          pyrrolidone                                                                   CTC             +      +        +     CTCI                                    Water/minors    Up to 100%                                                    ______________________________________                                         *The level of enzyme(s) is by weight of "pure" enzyme                         **to control pH                                                          

EXAMPLE 7

Granular fabric cleaning compositions in accordance with the inventionwere prepared as follows:

    ______________________________________                                        LAS                 6.5    8.0                                                Sulfate             15.0   18.0                                               Zeolite A           30.0   25.0                                               Sodium nitrilotriacetate                                                                          5.0    5.0                                                PVP                 0.5    0.7                                                Boric acid          4.0    --                                                 Silicate            5.0    5.0                                                Carbonate           15.0   15.0                                               * Protease          0.06   0.02                                               * Lipolytic enzyme(s)                                                                             0.01   0.01                                               * Amylase           0.01   0.01                                               * Cellulase (1000 CEVU/g)                                                                         0.6    0.8                                                CTC                 +      +                                                  Water/minors        Up to 100%                                                ______________________________________                                         *The level of enzyme(s) is by weight of "pure" enzyme                    

EXAMPLE 8

Compact granular fabric cleaning compositions in accordance with theinvention was prepared as follows:

    ______________________________________                                        45AS                 8.0     8.0                                              25E3S                2.0     2.0                                              25E5                 3.0     3.0                                              25E3                 3.0     3.0                                              TFAA                 2.5     2.5                                              Zeolite A            27.0    20                                               NaSKS-6              12.0    10                                               Citric acid/Citrate**                                                                              10.0    10                                               Carbonate            7.0     5                                                MA/AA                5.0     4                                                CMC                  0.4     0.4                                              Poly (4-vinylpyridine)-N-oxide/                                                                    0.2     0.2                                              copolymer of vinylimidazole and                                               vinylpyrrolidone                                                              Crosslinked poly(4-vinylpyridine)-N-                                                               --       0.2                                             oxide                                                                         * Protease           0.05    0.05                                             * Lipolytic enzyme(s)                                                                              0.005   0.005                                            * Cellulase          0.5     0.5                                              * Amylase            0.01    0.01                                             * Xylanase           0.05    0.05                                             EDDS                 0.3     0.3                                              Granular suds suppressor                                                                           3.5     3.5                                              CTC                  +       +                                                Water/minors         Up to 100%                                               ______________________________________                                         *The level of enzyme(s) is by weight of "pure" enzyme                         **to control pH                                                          

EXAMPLE 9

A granular fabric cleaning compositions in accordance with the inventionwhich provide "softening through the wash" capability were prepared asfollows:

    ______________________________________                                        45AS             --        10.0    --                                         LAS              7.6       --      7.6                                        68AS             1.3       --      1.3                                        45E7             4.0       --      2.0                                        25E3             --        5.0     3.0                                        Coco-alkyl-dimethyl hydroxy-                                                                   1.4       1.0     --                                         ethyl ammonium chloride                                                       Choline ester    --        --      1.5                                        Citrate/Citric acid**                                                                          8.0       15.0    12                                         Na-SKS-6         --        11.0    3                                          Zeolite A        15.0      15.0    15                                         MA/AA            4.0       4.0     4                                          DETPMP           0.4       0.4     0.4                                        Smectite clay    10.0      10.0    10                                         HMWPEO           --        0.1     0.2                                        * Protease       0.02      0.01    0.01                                       * Lipolytic enzyme(s)                                                                          0.02      0.01    0.02                                       * Amylase        0.03      0.005   0.03                                       * Cellulase (1000 CEVU/g)                                                                      0.5       0.5     0.6                                        Silicate         3.0       5.0     3.0                                        Carbonate        10.0      10.0    8.0                                        Granular suds suppressor                                                                       1.0       4.0     2.0                                        CMC              0.2       0.1     0.1                                        CTC              +         +       +                                          Water/minors     Up to 100%                                                   ______________________________________                                         *The level of enzyme(s) is by weight of "pure" enzyme                         **to control pH                                                          

EXAMPLE 10

Heavy duty liquid fabric cleaning compositions suitable for use in thepretreatment of stained fabrics, and for use in a machine launderingmethod, in accordance with the invention were prepared as follows:

    ______________________________________                                                   I      II      III     IV   V                                      ______________________________________                                        24AS         20.0     20.0    20.0  20.0 20.0                                 SS           5.0      5.0     5.0   5.0  5.0                                  Citrate      1.0      1.0     1.0   1.0  1.0                                  12E.sub.3    13.0     13.0    13.0  13.0 13.0                                 Monethanolamine                                                                            2.5      2.5     2.5   2.5  2.5                                  * Protease   0.005    0.03    0.02  0.04 0.01                                 * Lipolytic enzyme(s)                                                                      0.002    0.01    0.02  --   0.004                                * Amylase    0.005    0.005   --    --   0.004                                * Cellulase (1000 cevu/g                                                                   0.5      0.5-    0.6   0.6  0.8                                  * Pectinase  --       0.02    --    --   0.02                                 * Xylanase   --       --      --    --   0.03                                 CTC          +        +       +     +    +                                    Water/propylene                                                               glycol/ethanol                                                                (100:1:1)                                                                     ______________________________________                                         *The level of enzyme(s) is by weight of "pure" enzyme                    

EXAMPLE 11

Heavy duty liquid fabric cleaning compositions in accordance with theinvention were prepared as follows:

    ______________________________________                                                     I     II        III    IV                                        ______________________________________                                        LAS acid form  --      --        25.0 --                                      C.sub.12-14 alkenyl succinic                                                                 3.0     8.0       10.0 --                                      acid                                                                          Citric acid    10.0    15.0      2.0  2.0                                     25AS acid form 8.0     8.0       --   15.0                                    25AE2S acid form                                                                             --      3.0       --   4.0                                     25AE7          --      8.0       --   6.0                                     25AE3          8.0     --        --   --                                      CFAA           --      --        --   6.0                                     DETPMP         0.2     --        1.0  1.0                                     Fatty acid     --      --        --   10.0                                    Oleic acid     1.8     --        1.0  --                                      Ethanol        4.0     4.0       6.0  2.0                                     Propanediol    2.0     2.0       6.0  10.0                                    * Protease     0.02    0.02      0.02 0.01                                    * Lipolytic enzyme(s)                                                                        0.01    0.005     --   0.01                                    * Amylase      0.005   0.01      --   0.01                                    * Cellulase (1000 cevu/ml)                                                                   0.5     0.4       0.4  0.5                                     * Pectinase    0.02    --        --   --                                      * Xylanase     0.05    --        --   --                                      Coco-alkyl dimethyl                                                                          --      --        3.0  --                                      hydroxy ethyl ammonium                                                        chloride                                                                      Smectite clay  --      --        5.0  --                                      PVP            1.0     2.0       --   --                                      CTC            +       +         +    +                                       NaOH           Up to pH 7.5                                                   Waters/minors  Up to 100%                                                     ______________________________________                                         *The level of enzyme(s) is by weight of "pure" enzyme                    

    ______________________________________                                                       Additive Product                                                              I     II                                                       ______________________________________                                        Cellulase        20      25                                                   POD              20      15                                                   Enhancer CPPT     5       8                                                   Perborate        20      --                                                   Percarbonate     --      20                                                   Citric acid       5       5                                                   Filler           Up to 100%                                                   ______________________________________                                    

EXAMPLE 12

What is claimed is:
 1. A detergent composition comprising(i) cellulase;(ii) cellulase terminator composition comprisinga) a peroxidase; b) anenhancer, wherein the enhancer is incorporated into a release agent; c)a source of hydrogen peroxide characterized in that the activity of thecellulase is controlled in such a way that the activity of the cellulaseis more than 90% within 5 minutes from the start of the wash cycle, thecellulase activity is less than 50% within 5 to 10 minutes from thestart of the wash cycle and that less than 10% of residual cellulaseactivity is reached after 15 minutes in the wash cycle.
 2. A detergentcomposition according to claim 1, wherein one or more of the compoundsa) and c) is incorporated into a release agent.
 3. A detergentcomposition according to claim 1 wherein said cellulase is 43 kDendoglucanase derived from Humicola insolens, DSM
 1800. 4. A detergentcomposition according to claims 1 wherein the source of hydrogenperoxide is a peroxygen bleach including percarbonates and perborates.5. A detergent composition according to claim 1 wherein said enhancer is10-phenothiazinepropionic acid (PPT), 10-ethylphenothiazine-4-carboxylicacid (EPC), 10-phenoxazinepropionic acid (POP).
 6. A detergentcomposition according to claim 1 further comprising anionic surfactantsand nonionic surfactants.
 7. A detergent composition according to claim6 wherein the weight ratio of anionic to nonionic is between 10:1 to1:2.
 8. A detergent composition according to claim 1 wherein the pH isbetween 8 to
 10. 9. A detergent composition according to claim 1 furthercomprising a protease.
 10. A detergent composition according to claim 1further comprising a clay.
 11. A detergent composition according toclaim 1 further comprising a cationic surfactant.
 12. A detergentcomposition according to claim 1 further comprising a protease.
 13. Adetergent composition according to claim 1 which is in the form of aliquid, granular, gel, paste or bar.
 14. A detergent additive whichcomprises the detergent composition of claim
 1. 15. A detergentcomposition comprising(i) cellulase; (ii) cellulase terminatorcomposition comprisinga) a peroxidase; b) an enhancer wherein theenhancer is incorporated into a release agent; c) a source of hydrogenperoxide characterized in that the activity of the cellulase iscontrolled in such a way that the activity of the cellulase is more than90% within 5 minutes from the start of the wash cycle, the cellulaseactivity is less than 50% within 5 to 10 minutes from the start of thewash cycle and that less than 10% of residual cellulase activity isreached after 15 minutes in the wash cycle; and (iii) a surfactantsystem comprising sodium linear C₁₂ alkylbenzenesulfonate.